T. Meyer

发表

Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein

J. V. Van Beeumen, J. Kyndt, T. Meyer, 2002, FEBS letters.

Redox protein electron-transfer mechanisms: electrostatic interactions as a determinant of reaction site in c-type cytochromes.

G. Tollin, C. Stout, T. Meyer, 1989, Biochemistry.

Discovery and characterization of electron transfer proteins in the photosynthetic bacteria

T. Meyer, M. Cusanovich, 2004, Photosynthesis Research.

Discovery and characterization of electron transfer proteins in the photosynthetic bacteria

T. Meyer, M. Cusanovich, 2003 .

Discovery and characterization of electron transfer proteins in the photosynthetic bacteria 1

T. Meyer, M. Cusanovich, D. Keilin, 2003 .

Iron protein content of Thiocapsapfennigii, a purple sulfur bacterium of atypical chlorophyll composition.

S. Kennel, T. Meyer, S. Tedro, 1973, Biochimica et biophysica acta.

Protein dynamics: imidazole binding to class I C-type cytochromes.

T. Meyer, M. Cusanovich, C. Dumortier, 1999, Archives of biochemistry and biophysics.

Elucidation of the factors which determine reaction-rate constants and biological specificity for electron-transfer proteins.

G. Tollin, T. Meyer, M. Cusanovich, 1986, Biochimica et biophysica acta.

Preparation and properties of a 3,4-dihydroxycinnamic acid chromophore variant of the photoactive yellow protein.

E. Getzoff, G. Tollin, T. Meyer, 1997, Archives of biochemistry and biophysics.

Electron transfer proteins of the purple phototrophic bacterium, Rhodopseudomonas rutila.

J. V. Van Beeumen, T. Meyer, M. Cusanovich, 1991, Archives of biochemistry and biophysics.

Unusual high redox potential ferredoxins and soluble cytochromes from the moderately halophilic purple phototrophic bacterium Rhodospirillum salinarum

T. Meyer, M. Cusanovich, R. G. Bartsch, 1990 .

Expression of a cytochrome c2 isozyme restores photosynthetic growth of Rhodobacter sphaeroides mutants lacking the wild-type cytochrome c2 gene.

T. Donohue, G. Tollin, J. V. Van Beeumen, 1989, Archives of biochemistry and biophysics.

Kinetics of reduction by free flavin semiquinones of algal cytochromes and plastocyanin.

G. Tollin, T. Meyer, M. Cusanovich, 1987, Archives of biochemistry and biophysics.

Effects of pH and exocyclic substitution on flavosemiquinone reactivity with redox proteins and inorganic oxidants.

G. Tollin, T. Meyer, M. Cusanovich, 1985, Archives of biochemistry and biophysics.

pH dependence of the oxidation-reduction potential of cytochrome c2.

T. Meyer, R. G. Bartsch, G. Pettigrew, 1976, Biochimica et biophysica acta.

Transient kinetics of intracomplex electron transfer in the human cytochrome b5 reductase-cytochrome b5 system: NAD+ modulates protein-protein binding and electron transfer.

G. Tollin, M. Bes, T. Meyer, 1995, Archives of biochemistry and biophysics.

The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy

J. Sanders-Loehr, T. Meyer, M. Cusanovich, 1991 .

Reversible super-reduction of the cubane [4Fe-4S](3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions: EPR spectroscopic and electrochemical studies.

H. Heering, W. Hagen, T. Meyer, 1995 .

Reversible super-reduction of the cubane [4Fe-4S](3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions. EPR spectroscopic and electrochemical studies.

H. Heering, W. Hagen, T. Meyer, 1995, European journal of biochemistry.

Active site mutants implicate key residues for control of color and light cycle kinetics of photoactive yellow protein.

E. Getzoff, G. Tollin, T. Meyer, 1997, Biochemistry.

Redox potentials of the photosynthetic bacterial cytochromes c2 and the structural bases for variability.

T. Meyer, R. G. Bartsch, G. Pettigrew, 1978, Biochimica et biophysica acta.

A reassessment of the structure of Paracoccus cytochrome c-550.

S. Schichman, L. Sawyer, T. Meyer, 1981, Journal of molecular biology.

Picosecond decay kinetics and quantum yield of fluorescence of the photoactive yellow protein from the halophilic purple phototrophic bacterium, Ectothiorhodospira halophila.

G. Tollin, Robert Eugene Blankenship, P. Cheng, 1991, Biophysical journal.

GHP, a new c‐type green heme protein from Halochromatium salexigens and other proteobacteria

J. V. Van Beeumen, B. Devreese, T. Meyer, 2006, The FEBS Journal.

The complete amino acid sequence of rubredoxin from the green phototrophic bacterium Chlorobium thiosulphatophilum strain PM.

K. J. Woolley, T. Meyer, 1987, European journal of biochemistry.

Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin.

G. Tollin, T. Meyer, M. Cusanovich, 1993, Biochemistry.

Evolution of photosynthetic reaction centers and light harvesting chlorophyll proteins.

T. Meyer, 1994, Bio Systems.

Amino acid sequences of bacterial cytochromes c' and c-556.

J. V. Van Beeumen, L. McLellan, T. Meyer, 1981, Proceedings of the National Academy of Sciences of the United States of America.

A Heme-binding Protein from Hemolymph and Oocytes of the Blood-sucking Insect, Rhodnius prolixus

R. Poorman, F. Walker, J. Ribeiro, 1995, The Journal of Biological Chemistry.

Correlation between rate constant for reduction and redox potential as a basis for systematic investigation of reaction mechanisms of electron transfer proteins.

J. A. Watkins, G. Tollin, A. Bhattacharyya, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Isolation, characterization, and amino acid sequences of auracyanins, blue copper proteins from the green photosynthetic bacterium Chloroflexus aurantiacus.

G. Tollin, Robert Eugene Blankenship, D. Brune, 1992, The Journal of biological chemistry.

Amino acid sequences of two high-potential iron-sulfur proteins (HiPIPs) from the moderately halophilic purple phototrophic bacterium, Rhodospirillum salinarum.

T. Meyer, M. Cusanovich, M. Daniel, 1999, Archives of biochemistry and biophysics.

Cytochromes, Iron-Sulfur, and Copper Proteins Mediating Electron Transfer from the Cyt bc 1 Complex to Photosynthetic Reaction Center Complexes

T. Donohue, T. Meyer, 1995 .

Amino acid sequences of Euglena viridis ferredoxin and cytochromes c.

T. Meyer, R. Ambler, R. G. Bartsch, 1991, The Biochemical journal.

Genome Sequence and Characterization of a Xanthorhodopsin-Containing, Aerobic Anoxygenic Phototrophic Rhodobacter Species, Isolated from Mesophilic Conditions at Yellowstone National Park

J. Kyndt, T. Meyer, R. Ramaley, 2022, Microorganisms.

Plasmon waveguide resonance spectroscopic evidence for differential binding of oxidized and reduced Rhodobacter capsulatus cytochrome c2 to the cytochrome bc1 complex mediated by the conformation of the Rieske iron-sulfur protein.

Z. Salamon, G. Tollin, E. Berry, 2007, Biochemistry.

EPR analysis of multiple forms of [4Fe–4S]3+ clusters in HiPIPs

F. Capozzi, C. Luchinat, W. Hagen, 2005, JBIC Journal of Biological Inorganic Chemistry.

Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentans.

G. Tollin, S. Ciurli, A. Hochkoeppler, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Influence of charge and polarity on the redox potentials of high-potential iron-sulfur proteins: evidence for the existence of two groups.

H. Heering, W. Hagen, T. Meyer, 1995, Biochemistry.

Purification and properties of high-potential iron-sulfur proteins.

T. Meyer, 1994, Methods in enzymology.

Amino acid sequence of a high redox potential ferredoxin (HiPIP) from the purple phototrophic bacterium Rhodopila globiformis, which has the highest known redox potential of its class.

T. Meyer, M. Kamen, R. Ambler, 1993, Archives of biochemistry and biophysics.

Amino acid sequence of high-redox-potential ferredoxin (HiPIP) isozymes from the extremely halophilic purple phototrophic bacterium, Ectothiorhodospira halophila.

T. Meyer, S. Tedro, M. Kamen, 1985, Archives of biochemistry and biophysics.

Primary structures of high potential, four-iron-sulfur ferredoxins from the pruple sulfur photosynthetic bacteria, Thiocapsa roseopersicina and chromatium gracile.

T. Meyer, R. G. Bartsch, S. Tedro, 1981, The Journal of biological chemistry.

Primary structure of a high potential iron sulfur protein from a moderately halophilic denitrifying coccus.

T. Meyer, M. Kamen, S. Tedro, 1977, The Journal of biological chemistry.

Purification, properties and amino acid sequence of atypical cytochrome c from two protozoa, Euglena gracilis and Crithidia oncopelti.

T. Meyer, G. Pettigrew, J. Leaver, 1975, The Biochemical journal.

Primary structure of a high potential iron-sulfur protein from the photosynthetic bacterium Thiocapsa pfennigii.

T. Meyer, S. Tedro, M. Kamen, 1974, The Journal of biological chemistry.

The major soluble cytochromes of the obligately aerobic sulfur bacterium, Thiobacillus neapolitanus

T. Meyer, R. G. Bartsch, M. Kamen, 1985, Archives of Microbiology.

Isolation and properties of rubredoxin from the photosynthetic green sulfur bacteria.

T. Meyer, R. G. Bartsch, J. J. Sharp, 1971, Biochimica et biophysica acta.

The cytochromes of Chlorobium thiosulfatophilum.

J. Mathewson, T. Meyer, M. Cusanovich, 1968, Biochimica et biophysica acta.

Heterologous production of Halorhodospira halophila holo-photoactive yellow protein through tandem expression of the postulated biosynthetic genes.

J. V. Van Beeumen, B. Devreese, J. Kyndt, 2003, Biochemistry.

Evolution of cytochromes and photosynthesis.

T. Meyer, 1991, Biochimica et biophysica acta.

Soluble cytochromes and a photoactive yellow protein isolated from the moderately halophilic purple phototrophic bacterium, Rhodospirillum salexigens.

G. Tollin, T. Meyer, M. Cusanovich, 1990, Biochimica et biophysica acta.

In vitro kinetics of reduction of cytochrome c554 isolated from the reaction center of the green phototrophic bacterium, Chloroflexus aurantiacus.

G. Tollin, J. Freeman, Robert Eugene Blankenship, 1989, Archives of biochemistry and biophysics.

Regulation of a cytochrome c2 isoform in wild-type and cytochrome c2 mutant strains of Rhodobacter sphaeroides.

T. Donohue, T. Meyer, J. Fitch, 1992, Archives of biochemistry and biophysics.

The genome sequence of the giant phototrophic gammaproteobacterium Thiospirillum jenense gives insight into its physiological properties and phylogenetic relationships

J. Imhoff, J. Kyndt, T. Meyer, 2020, Archives of Microbiology.

The amino acid sequence of the cytochrome c-554(547) from the chemolithotrophic bacterium Thiobacillus neapolitanus.

T. Meyer, M. Kamen, P. Trudinger, 1985, The Biochemical journal.

Coupling of hydrogen bonding to chromophore conformation and function in photoactive yellow protein.

E. Getzoff, G. Tollin, K. Gerwert, 2000, Biochemistry.

CYTOCHROMES AND FERREDOXINS IN BACTERIAL ELECTRON TRANSPORT AND CLASSIFICATION

T. Meyer, 1982 .

Protein dynamics: imidazole and 2-mercaptoethanol binding to the Rhodobacter capsulatus cytochrome c(2) mutant, glycine 95 proline.

T. Meyer, M. Cusanovich, C. Dumortier, 2002, Archives of biochemistry and biophysics.

1H and 13C NMR assignment and secondary structure of Chlorobium limicola f. thiosulfatophilum ferrocytochrome c 555

J. Simorre, D. Marion, M. Caffrey, 1995, FEBS letters.

Structure of cytochrome c′: a dimeric, high-spin haem protein

N. Xuong, R. Hamlin, P. Weber, 1980, Nature.

Amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1.

T. Meyer, R. Ambler, R. G. Bartsch, 1975, The Journal of biological chemistry.

New perspectives on c-type cytochromes.

T. Meyer, M. Kamen, Terrance E. Meyer, 1982, Advances in protein chemistry.

The amino acid sequence of cytochrome c' from the purple sulphur bacterium Chromatium vinosum.

T. Meyer, R. G. Bartsch, M. Kamen, 1979, The Biochemical journal.

Kinetics of reduction of high redox potential ferredoxins by the semiquinones of Clostridium pasteurianum flavodoxin and exogenous flavin mononucleotide. Electrostatic and redox potential effects.

G. Tollin, T. Meyer, M. Cusanovich, 1985, Biochemistry.

Transient kinetics of reduction of blue copper proteins by free flavin and flavodoxin semiquinones.

E. Getzoff, G. Tollin, T. Meyer, 1986, Biochemistry.

Direct measurement of intramolecular electron transfer between type I and type III copper centers in the multi-copper enzyme ascorbate oxidase and its type II copper-depleted and cyanide-inhibited forms.

G. Tollin, T. Meyer, M. Cusanovich, 1991, Biochemistry.

Reduction kinetics of the ferredoxin-ferredoxin-NADP+ reductase complex: a laser flash photolysis study.

G. Tollin, T. Meyer, A. Bhattachryya, 1986, Biochemistry.

Adduct formation between sulfite and the flavin of phototrophic bacterial flavocytochromes c. Kinetics of sequential bleach, recolor, and rebleach of flavin as a function of pH.

T. Meyer, M. Cusanovich, R. G. Bartsch, 1991, Biochemistry.

Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila.

T. Meyer, T E Meyer, Terrance E. Meyer, 1985, Biochimica et biophysica acta.

Use of laser flash photolysis time-resolved spectrophotometry to investigate interprotein and intraprotein electron transfer mechanisms.

G. Tollin, T. Meyer, J. K. Hurley, 1993, Biophysical chemistry.

Electron transfer between flavodoxin semiquinone and c-type cytochromes: correlations between electrostatically corrected rate constants, redox potentials, and surface topologies.

J. A. Watkins, G. Tollin, T. Meyer, 1984, Biochemistry.

Electron-transfer reactions of photoreduced flavin analogues with c-type cytochromes: quantitation of steric and electrostatic factors.

J. A. Watkins, G. Tollin, T. Meyer, 1984, Biochemistry.

On the monohene character of cytochromes c'.

S. Kennel, T. Meyer, R. G. Bartsch, 1972, Proceedings of the National Academy of Sciences of the United States of America.

Soluble cytochromes and ferredoxins from the marine purple phototrophic bacterium, Rhodopseudomonas marina.

G. Tollin, T. Meyer, M. Cusanovich, 1990, Biochimica et biophysica acta.

applied to electron transfer proteins A ` ` parallel plate ' ' electrostatic model for bimolecular rate constants

G. Tollin, T. Meyer, M. Cusanovich, 2002 .

A “parallel plate” electrostatic model for bimolecular rate constants applied to electron transfer proteins

J. A. Watkins, G. Tollin, T. Meyer, 1994, Protein science : a publication of the Protein Society.

Effect of aerobic growth conditions on the soluble cytochrome content of the purple phototrophic bacterium Rhodobacter sphaeroides: induction of cytochrome c554.

T. Meyer, M. Cusanovich, R. G. Bartsch, 1989, Archives of biochemistry and biophysics.

A directional electron transfer regulator based on heme‐chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis

K. Nealson, A. Tsapin, K. Ozawa, 2002, FEBS letters.

Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore

K. Hellingwerf, D. McRee, J. V. Van Beeumen, 1993, Protein science : a publication of the Protein Society.

Anomalies in amino acid sequences of small cytochromes c and cytochromes c′ from two species of purple photosynthetic bacteria

T. Meyer, M. Kamen, R. Ambler, 1979, Nature.

Evolutionary Analysis by Whole-Genome Comparisons

Arvind K. Bansal, A. Bansal, T. Meyer, 2002, Journal of bacteriology.

Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery.

G. Tollin, T. Meyer, M. Cusanovich, 1989, Biophysical journal.

Structure and Characterization of Ectothiorhodospira vacuolata Cytochrome b 558, a Prokaryotic Homologue of Cytochrome b 5 *

J. V. Van Beeumen, Y. Guisez, D. Leys, 1999, The Journal of Biological Chemistry.

Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.

J. Kraut, G. Tollin, T. Meyer, 1988, Biochemistry.

A Membrane-Bound Flavocytochromec-Sulfide Dehydrogenase from the Purple Phototrophic Sulfur Bacterium Ectothiorhodospira vacuolata

J. V. Van Beeumen, Y. Guisez, T. Meyer, 2000, Journal of bacteriology.

Kinetics of electron transfer from thioredoxin reductase to thioredoxin.

G. Tollin, J. Fuchs, F. K. Gleason, 1991, Biochemistry.

Structural and Functional Diversity Among Bacterial Electron Transport Protein

T. Meyer, M. Kamen, 1982 .

Metal coordination centres of class II cytochromes c.

R. J. Williams, P. Tempst, J. V. Van Beeumen, 1982, European journal of biochemistry.

Laser flash photolysis studies of electron transfer to the cytochrome b5-cytochrome c complex.

G. Tollin, M. Rivera, F. Walker, 1993, Biochemistry.

Electron-transfer reactions between flavodoxin semiquinone and c-type cytochromes: comparisons between various flavodoxins.

G. Tollin, C. Stout, T. Meyer, 1986, Biochemistry.

Comparative Genome Analysis of the Photosynthetic Betaproteobacteria of the Genus Rhodocyclus: Heterogeneity within Strains Assigned to Rhodocyclus tenuis and Description of Rhodocyclus gracilis sp. nov. as a New Species

J. Imhoff, S. Künzel, J. Kyndt, 2022, Microorganisms.

Cytochromes C2 sequence variation among the recognised species of purple nonsulphur photosynthetic bacteria

T. Meyer, J. Hermoso, M. Kamen, 1979, Nature.

The amino acid sequences of the cytochromes c-555 from two green sulphur bacteria of the genus Chlorobium.

J. Olson, J. V. Van Beeumen, T. Meyer, 1976, The Biochemical journal.

Cytochrome c3. A class of electron transfer heme proteins found in both photosynthetic and sulfate-reducing bacteria

Martin D. Kamen, T. Meyer, R. G. Bartsch, 1971 .

Complex formation between Chlorobium limicola f. thiosulfatophilumc-type cytochromes

T. Meyer, M. Cusanovich, D. Knaff, 1986 .

Protein interaction sites obtained via sequence homology. The site of complexation of electron transfer partners of cytochrome c revealed by mapping amino acid substitutions onto three-dimensional protein surfaces.

G. Tollin, T. Meyer, M. Cusanovich, 1994, Biochimie.

Characterization of Glutathione Amide Reductase from Chromatium gracile

J. V. Van Beeumen, T. Meyer, B. Vergauwen, 2001, The Journal of Biological Chemistry.

The genome sequence of the giant phototrophic gammaproteobacterium Thiospirillum jenense gives insight into its physiological properties and phylogenetic relationships

J. Imhoff, J. Kyndt, T. Meyer, 2020, Archives of Microbiology.

New insights into the photocycle of Ectothiorhodospira halophila photoactive yellow protein: photorecovery of the long-lived photobleached intermediate in the Met100Ala mutant.

E. Getzoff, G. Tollin, T. Meyer, 1998, Biochemistry.

An alternative to the accepted phylogeny of purple bacteria based on 16S rRNA: analyses of the amino acid sequences of cytochromes C2 and C556 from Rhodobacter (Rhodovulum) sulfidophilus.

T. Meyer, M. Cusanovich, R. G. Bartsch, 2001, Archives of biochemistry and biophysics.

Evidence against use of bacterial amino acid sequence data for construction of all-inclusive phylogenetic trees.

T. Meyer, M. Cusanovich, M. Kamen, 1986, Proceedings of the National Academy of Sciences of the United States of America.

Use of flavin and flavodoxin semiquinones as kinetic probes to elucidate the factors which determine reaction rate constants and biological specificity for electron transfer proteins

G. Tollin, T. Meyer, M. Cusanovich, 1987 .

Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus determined at 2.5 A resolution.

I. Rayment, H. Holden, M. Benning, 1991, Journal of molecular biology.

Photobleaching of the photoactive yellow protein from Ectothiorhodospira halophila promotes binding to lipid bilayers: evidence from surface plasmon resonance spectroscopy.

Z. Salamon, G. Tollin, T. Meyer, 1995, Biophysical journal.

Phylogenetic relationship of phototrophic heliobacteria and systematic reconsideration of species and genus assignments based on genome sequences of eight species.

J. Imhoff, J. Kyndt, T. Meyer, 2021, International journal of systematic and evolutionary microbiology.

Primary structure determination of two cytochromes c2: close similarity to functionally unrelated mitochondrial cytochrome C.

T. Meyer, M. Kamen, R. Ambler, 1976, Proceedings of the National Academy of Sciences of the United States of America.

Comparative Cytochrome c Biochemistry

T. Meyer, M. Kamen, 1981 .

Redox pathways in electron-transfer proteins: correlations between reactivities, solvent exposure, and unpaired-spin-density distributions.

L. K. Hanson, G. Tollin, M. Caffrey, 1986, Proceedings of the National Academy of Sciences of the United States of America.

Genomic Comparison, Phylogeny and Taxonomic Reevaluation of the Ectothiorhodospiraceae and Description of Halorhodospiraceae fam. nov. and Halochlorospira gen. nov.

J. Imhoff, J. Kyndt, T. Meyer, 2022, Microorganisms.

Primary structure determination of two cytochromes c2: close similarity to functionally unrelated mitochondrial cytochrome C.

T. Meyer, M. Kamen, R. Ambler, 1976, Proceedings of the National Academy of Sciences of the United States of America.

The amino acid sequence of a high-redox-potential ferredoxin from the purple phototrophic bacterium, Rhodospirillum tenue strain 2761.

T. Meyer, S. Tedro, M. Kamen, 1985, Archives of biochemistry and biophysics.

Purification and properties of cytochrome c-555 from phototrophic green sulfur bacteria.

T. Meyer, 1994, Methods in enzymology.

The question of histidine content in c-type cytochromes.

T. Meyer, M. Cusanovich, S. Tedro, 1971, Proceedings of the National Academy of Sciences of the United States of America.

Crystal Structures of an Oxygen-binding Cytochrome cfrom Rhodobacter sphaeroides *

J. V. Van Beeumen, W. Hagen, D. Leys, 2000, The Journal of Biological Chemistry.

Correlation between rateconstant forreduction andredox potential asabasis forsystematic investigation ofreaction mechanisms ofelectron transfer proteins (cytochromes/ferredoxins/metalloproteins/flavins /copper proteins)

J. A. Watkins, A. Bhattacharyya, T. Meyer, 1983 .

Amino acid sequences of cytochromes c2 and c' from the moderately halophilic purple phototrophic bacterium Rhodospirillum salexigens.

T. Meyer, M. Kamen, M. Daniel, 1994, Biochimie.

Oxidative turnover increases the rate constant and extent of intramolecular electron transfer in the multicopper enzymes, ascorbate oxidase and laccase.

G. Tollin, T. Meyer, M. Cusanovich, 1993, Biochimica et biophysica acta.

Kinetics of photooxidation of soluble cytochromes, HiPIP, and azurin by the photosynthetic reaction center of the purple phototrophic bacterium Rhodopseudomonas viridis.

G. Tollin, T. Meyer, M. Cusanovich, 1993, Biochemistry.

Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash photolysis.

Z. Salamon, G. Tollin, J. Markley, 1993, Biochemistry.

Transient proton uptake and release is associated with the photocycle of the photoactive yellow protein from the purple phototrophic bacterium Ectothiorhodospira halophila.

G. Tollin, T. Meyer, M. Cusanovich, 1993, Archives of biochemistry and biophysics.

Amino acid sequences of cytochromes c-551 from the halophilic purple phototrophic bacteria, Ectothiorhodospira halophila and E. halochloris.

T. Meyer, M. Kamen, R. Ambler, 1993, Archives of biochemistry and biophysics.

Primary structure of a high potential, four-iron-sulfur ferredoxin from the photosynthetic bacterium Rhodospirillum tenue.

T. Meyer, S. Tedro, M. Kamen, 1979, The Journal of biological chemistry.

Primary structure of a high potential iron-sulfur protein from the purple non-sulfur photosynthetic bacterium Rhodopseudomonas gelatinosa.

T. Meyer, S. Tedro, M. Kamen, 1976, The Journal of biological chemistry.

Amino acid sequences of two high-potential iron sulfur proteins (HiPIPs) from the moderately halophilic purple phototrophic bacterium Ectothiorhodospira vacuolata.

T. Meyer, M. Kamen, R. Ambler, 1994, Archives of biochemistry and biophysics.

The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium.

J. V. Van Beeumen, T. Meyer, Z. Chen, 1994, Science.

Characterization of Soluble Forms of the Membrane Bound Iso-Cytochrome c2 from Rhodobacter Capsulatus

G. Tollin, T. Meyer, M. Cusanovich, 1999 .

New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: picosecond transient absorption spectroscopy.

G H Atkinson, G. Tollin, T. Meyer, 1998, Biophysical journal.

Rhodobacter capsulatus photoactive yellow protein: genetic context, spectral and kinetics characterization, and mutagenesis.

G. Tollin, J. V. Van Beeumen, B. Devreese, 2004, Biochemistry.

Electron Transfer Mechanisms in Heme Proteins

G. Tollin, T. Meyer, M. Cusanovich, 1989 .

Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin.

J. V. Van Beeumen, T. Meyer, T. Meyer, 1993, The Journal of biological chemistry.

The amino acid sequence of the cytochrome c2 from the phototrophic bacterium Rhodopseudomonas globiformis.

T. Meyer, M. Cusanovich, R. Ambler, 1987, The Biochemical journal.