S. Chapman

发表

Determination of the redox properties of human NADPH-cytochrome P450 reductase.

A. Munro, M. Noble, L. Robledo, 2001, Biochemistry.

Redox control of the catalytic cycle of flavocytochrome P-450 BM3.

T. Poulos, A. Munro, S. Daff, 1997, Biochemistry.

Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria.

S. Chapman, F. B. Ward, S. L. Pealing, 1992, Biochemistry.

Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.

T. Ost, A. Munro, S. Chapman, 2001, Biochemistry.

Exploring the mechanism of tryptophan 2,3-dioxygenase

Sarah J. Thackray, S. Chapman, C. Mowat, 2008, Biochemical Society transactions.

ELECTRON-TRANSFER IN PROTEINS

A. Mount, S. Chapman, 1995 .

Rate constants for intramolecular electron-transfer reactions of ruthenium-modified histidine mutants of cytochrome b2

S. Chapman, G. Salmon, A. Sykes, 1994 .

Catalysis in fumarate reductase.

S. Chapman, R. Moysey, G. Reid, 2000, Biochimica et biophysica acta.

Fumarate reductase: Structural and mechanistic insights from the catalytic reduction of 2‐methylfumarate

M. Walkinshaw, S. Chapman, G. Reid, 2006, FEBS letters.

Redox properties of flavocytochrome c3 from Shewanella frigidimarina NCIMB400.

H. Heering, M. Doherty, F. Armstrong, 1999, Biochemistry.

Flavocytochrome b2: an ideal model system for studying protein-mediated electron transfer.

S. Daff, S. Chapman, G. Reid, 1996, Biochemical Society transactions.

Physiological function and regulation of flavocytochrome c3, the soluble fumarate reductase from Shewanella putrefaciens NCIMB 400.

S. Chapman, S. L. Pealing, G. Reid, 1998, Microbiology.

Probing the substrate specificity of the catalytically self-sufficient cytochrome P450 RhF from a Rhodococcus sp.

John H. White, S. Chapman, N. Turner, 2006, Chemical communications.

Flavocytochrome b 2

S. Chapman, C. Mowat, 2000 .

Purification and properties of a novel cytochrome: flavocytochrome c from Shewanella putrefaciens.

S. Chapman, C. Morris, D. Gibson, 1994, The Biochemical journal.

Electron-transfer mechanisms through biological redox chains in multicenter enzymes.

F. Armstrong, S. Chapman, G. Cecchini, 2002, Journal of the American Chemical Society.

Re-design of Saccharomyces cerevisiae flavocytochrome b2: introduction of L-mandelate dehydrogenase activity.

S. Chapman, G. Reid, R. Sinclair, 1998, The Biochemical journal.

Strategic manipulation of the substrate specificity of Saccharomyces cerevisiae flavocytochrome b2.

S. Daff, S. Chapman, F. Manson, 1994, The Biochemical journal.

High-level expression of fully active yeast flavocytochrome b2 in Escherichia coli.

S. White, S. Chapman, G. Reid, 1989, The Biochemical journal.

L-Mandelate dehydrogenase from Rhodotorula graminis: cloning, sequencing and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain.

R. Illias, S. Chapman, A. Neu, 1998, The Biochemical journal.

Metal Sites in Proteins and Models: Redox Centres. H.A.O. Hill, P.J. Sadler and A.J. Thomson (eds). Springer, Heidelberg, 1998. 209 pages. £76. ISBN 3‐540‐62888‐6

S. Chapman, 1999 .

Molecular mechanisms of enzyme-catalysed halogenation.

S. Chapman, J. L. Anderson, 2006, Molecular bioSystems.

Cytochrome cd(1) from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior.

S. Chapman, K. Turner, S. Ferguson, 2000, Biochemistry.

Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

A. Munro, M. Noble, L. Robledo, 1999, Biochemistry.

On the difference between iron-molybdenum cofactor of wild-type and nifV mutant molybdenum-iron proteins of Klebsiella pneumoniae: ENDOR, EXAFS, and EPR evidence

S. Chapman, B. Hoffman, W. Orme-Johnson, 1987 .

The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis.

S. Chapman, G. Reid, C. Schwalb, 2003, Biochemistry.

Kinetic studies on 1:1 electron transfer reactions involving blue copper proteins: 8. Reactions of plastocyanin and azurin with cytochrome c and high potential iron-sulfur protein

S. Chapman, M. Augustin, A. D. Watson, 1984 .

Redox-active lipid-incorporating proteins as a novel immobilisation technique

S. Chapman, H. Hill, T. Booth, 1997 .

Interaction of cytochrome c with flavocytochrome b2.

S. Daff, S. Chapman, F. Manson, 1996, Biochemistry.

Potentiometric analysis of UDP-galactopyranose mutase: stabilization of the flavosemiquinone by substrate.

C. Whitfield, Stephen W B Fullerton, J. Naismith, 2003, Biochemistry.

The Chemistry of the Copper and Zinc Triads

S. Chapman, A. J. Welch, Zinc Triads, 1993 .

The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamily.

Kenneth A Johnson, James H Naismith, Robert S Phillips, 2007, Biochemistry.

Kinetic studies on 1 : 1 electron-transfer reactions involving blue copper proteins. Part 6. Competitive inhibition of the [Co(phen)3]3+(phen = 1,10-phenanthroline) oxidation of parsley plastocyanin PCu(I) by redox-inactive complexes

S. Chapman, A. D. Watson, A. Sykes, 1983 .

Preferred sites on cytochrome c for electron transfer with two positively charged blue copper proteins, Anabaena variabilis plastocyanin and stellacyanin.

E. Margoliash, N. Osheroff, A. Aitken, 1986, Biochemistry.

The nature of amide ligation to the metal sites of FeMoco

S. Chapman, W. Orme-Johnson, M. Walters, 1986 .

Preferred sites for electron transfer between cytochrome c and iron and cobalt complexes.

E. Margoliash, N. Osheroff, S. Chapman, 1983, The Journal of biological chemistry.

Heme: The most versatile redox centre in biology?

A. Munro, S. Daff, S. Chapman, 1997 .

Substitution of Tyr254 with Phe at the active site of flavocytochrome b2: consequences on catalysis of lactate dehydrogenation.

F. S. Mathews, F. Lederer, S. Chapman, 1990, Biochemistry.

Oxygen activation and electron transfer in flavocytochrome P450 BM3.

Jonathan P. Clark, T. Ost, M. Walkinshaw, 2003, Journal of the American Chemical Society.

Indoleamine 2,3‐Dioxygenase and Tryptophan 2,3‐Dioxygenase

Sarah J. Thackray, L. Tong, F. Forouhar, 2011 .

The NrfH Cytochrome c Quinol Dehydrogenase

Sarah J. Thackray, L. Tong, F. Forouhar, 2008 .

Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase

Sarah J. Thackray, G. Montelione, T. Acton, 2007, Proceedings of the National Academy of Sciences.

The Mechanism of Substrate Inhibition in Human Indoleamine 2,3-Dioxygenase

I. Efimov, S. Chapman, J. Basran, 2012, Journal of the American Chemical Society.

FLAVINS AND FLAVOPROTEINS 1993

R. E. Sharp, S. Daff, S. Chapman, 1994 .

Effects of environment on flavin reactivity in morphinone reductase: analysis of enzymes displaying differential charge near the N-1 atom and C-2 carbonyl region of the active-site flavin.

N. Scrutton, A. Munro, S. Chapman, 2001, The Biochemical journal.

Atomic Structure of Mycobacterium tuberculosis CYP121 to 1.06 Å Reveals Novel Features of Cytochrome P450*

Malcolm D. Walkinshaw, Stephen K. Chapman, Christopher G. Mowat, 2003, The Journal of Biological Chemistry.

Expression, purification and spectroscopic characterization of the cytochrome P450 CYP121 from Mycobacterium tuberculosis.

N. C. Price, A. Munro, S. Chapman, 2002, Journal of inorganic biochemistry.

Crystallographic study of the recombinant flavin-binding domain of Baker's yeast flavocytochrome b(2): comparison with the intact wild-type enzyme.

S. Chapman, L. Cunane, G. Reid, 2002, Biochemistry.

Mechanisms for regulating electron transfer in multi-centre redox proteins.

S. Chapman, R. Sharp, R.Eryl Sharp, 1999, Biochimica et biophysica acta.

Ligand probes for heme proteins.

S. Chapman, J. L. Anderson, 2005, Dalton transactions.

Interaction of cytochrome c with the blue copper proteins, plastocyanin and azurin.

E. Margoliash, S. Chapman, M. Augustin, 1983, Journal of Biological Chemistry.

Structural and mechanistic mapping of a unique fumarate reductase

P. Taylor, M. Walkinshaw, S. Chapman, 1999, Nature Structural Biology.

Probing electron transfer in flavocytochrome P-450 BM3 and its component domains.

J. Coggins, A. Munro, S. Daff, 1996, European journal of biochemistry.

Analysis of the domain properties of the novel cytochrome P450 RhF

John H. White, Nicholas J Turner, Dominic J. B. Hunter, 2005, FEBS letters.

A Self-sufficient Cytochrome P450 with a Primary Structural Organization That Includes a Flavin Domain and a [2Fe-2S] Redox Center*

John H. White, Nicholas J Turner, Dominic J. B. Hunter, 2003, Journal of Biological Chemistry.

Roles of key active-site residues in flavocytochrome P450 BM3.

A. Munro, M. Noble, S. Chapman, 1999, The Biochemical journal.

Protein engineering of cytochromes P-450.

T. Ost, A. Munro, M. Noble, 2000, Biochimica et biophysica acta.

P450 BM3: the very model of a modern flavocytochrome.

K. R. Marshall, T. Ost, P. Dutton, 2002, Trends in biochemical sciences.

Flavin-containing heme enzymes.

S. Chapman, Ben Gazur, C. Mowat, 2010, Archives of biochemistry and biophysics.

Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding.

Sarah J. Thackray, L. Tong, R. Xiao, 2008, Biochemistry.

Altered substrate specificity in flavocytochrome b2: structural insights into the mechanism of L-lactate dehydrogenation.

M. Walkinshaw, S. Chapman, G. Reid, 2004, Biochemistry.

Mutation to glutamine of histidine 373, the catalytic base of flavocytochrome b2 (L-lactate dehydrogenase).

F. Lederer, S. Chapman, F. Manson, 1995, Biochimie.

Structural basis for the kinetic differences between flavocytochromes b2 from the yeasts Hansenula anomala and Saccharomyces cerevisiae.

S. Chapman, G. Reid, M. T. Black, 1989, The Biochemical journal.

Probing the active site of flavocytochrome b2 by site-directed mutagenesis.

F. Lederer, S. White, S. Chapman, 1988, European journal of biochemistry.

Redox behaviour of the haem domain of flavocytochrome c 3 from Shewanella frigidimarina probed by NMR

S. Chapman, R. Louro, D. Turner, 2004, FEBS letters.

Tuning of functional heme reduction potentials in Shewanella fumarate reductases.

S. Chapman, R. Louro, D. Turner, 2009, Biochimica et biophysica acta.

Probing domain mobility in a flavocytochrome.

M. Walkinshaw, S. Chapman, G. Reid, 2004, Biochemistry.

Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina.

M. Walkinshaw, S. Chapman, G. Reid, 2003, Biochemistry.

Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3.

S. Chapman, I. Correia, R. Louro, 2003, The Biochemical journal.

Engineering water to act as an active site acid catalyst in a soluble fumarate reductase.

M. Walkinshaw, S. Chapman, D. Leys, 2002, Biochemistry.

Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina.

M. Walkinshaw, S. Chapman, D. Leys, 2002, Biochemistry.

NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem‐specific axial ligands and order of oxidation

S. Chapman, D. Turner, A. V. Xavier, 2001, FEBS letters.

Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study.

P. Taylor, M. Doherty, M. Walkinshaw, 2000, Biochemistry.

Interruption and Time-Resolution of Catalysis by a Flavoenzyme Using Fast Scan Protein Film Voltammetry

Graeme A. Reid, Fraser A. Armstrong, F. Armstrong, 2000 .

Structure and function of flavocytochrome c3, the soluble fumarate reductase from Shewanella NCIMB400.

M. Doherty, S. Chapman, K. Turner, 1998, Biochemical Society transactions.

Spectroscopic and kinetic studies of the tetraheme flavocytochrome c from Shewanella putrefaciens NCIMB400.

S. Chapman, A. Thomson, M. Cheesman, 1995, Biochemistry.

Role of the interdomain hinge of flavocytochrome b2 in intra- and inter-protein electron transfer.

S. Chapman, G. Reid, P. White, 1994, Biochemistry.

On the lack of coordination between protein folding and flavin insertion in Escherichia coli for flavocytochrome b2 mutant forms Y254L and D282N

F. Lederer, S. Chapman, M. Gondry, 1995, Protein science : a publication of the Protein Society.

The D282N and Y254L active-site mutants of flavocytochrome b2 are expressed in E. coli as a mixture of holoenzyme and flavin-free protein

F. Lederer, S. Chapman, M. Gondry, 1994 .

Tyr-143 facilitates interdomain electron transfer in flavocytochrome b2.

F. Lederer, S. Chapman, N. Rouvière-Fourmy, 1992, The Biochemical journal.

Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli.

R. Baxter, A. Munro, S. Daff, 1998, European journal of biochemistry.

αArg-237 in Methylophilus methylotrophus (sp. W3A1) Electron-transferring Flavoprotein Affords ∼200-Millivolt Stabilization of the FAD Anionic Semiquinone and a Kinetic Block on Full Reduction to the Dihydroquinone*

M. Sutcliffe, N. Scrutton, A. Munro, 2001, The Journal of Biological Chemistry.

Kinetic studies on the oxidation of calf liver cytochrome b5 with inorganic complexes

S. Chapman, D. M. Davies, A. Sykes, 1984 .

Probing the Ternary Complexes of Indoleamine and Tryptophan 2,3-Dioxygenases by Cryoreduction EPR and ENDOR Spectroscopy

Sarah J. Thackray, S. Chapman, B. Hoffman, 2010, Journal of the American Chemical Society.

Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

Katy J. Drewette, Paul Taylor, Lisa McIver, 2004, Nature Structural &Molecular Biology.

Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.

K. R. Marshall, A. Munro, M. Noble, 2004, Biochemistry.

Catalytic properties of key active site mutants of flavocytochrome P-450 BM3

A. Munro, M. Noble, S. Chapman, 1999 .

Reassessment of the reaction mechanism in the heme dioxygenases.

Sarah J. Thackray, I. Efimov, S. Chapman, 2009, Journal of the American Chemical Society.

A Proton Delivery Pathway in the Soluble Fumarate Reductase from Shewanella frigidimarina*

M. Walkinshaw, F. Armstrong, S. Chapman, 2006, Journal of Biological Chemistry.

Calmodulin Activates Electron Transfer through Neuronal Nitric-oxide Synthase Reductase Domain by Releasing an NADPH-dependent Conformational Lock*

S. Daff, S. Chapman, D. Craig, 2002, The Journal of Biological Chemistry.

Rational re‐design of the substrate binding site of flavocytochrome P450 BM3

T. Ost, A. Munro, S. Chapman, 2000, FEBS letters.

Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. Part 9. Effects of chromium(III) modification on reactions of plastocyanin with [Co(phen)3]3+(phen = 1,10-phenanthroline), [Fe(CN)6]3–, [Co(dipic)2]–(dipic = dipicolinate)(oxidants) and [Ru(NH3)5(py)]2+(py = pyridine)

S. Chapman, A. Sykes, P. Kathirgamanathan, 1984 .

The influence of charge on reactions of metalloproteins with small molecules

S. Chapman, A. Sykes, ROBERT J. P. Williams, 1983 .

Flavocytochrome P450 BM3 substrate selectivity and electron transfer in a model cytochrome P450.

T. Ost, A. Munro, M. Noble, 2000, Sub-cellular biochemistry.

Flavocytochromes: Nature’s Electrical Transformers

A. Munro, S. Chapman, G. Reid, 1998 .

Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration.

S. Chapman, G. Reid, E. Gordon, 2000, The Biochemical journal.

Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase.

S K Chapman, A W Munro, N. C. Price, 2000, The Biochemical journal.

Flavocytochromes: transceivers and relays in biological electron transfer.

S K Chapman, F Welsh, R Moysey, 1999, Biochemical Society transactions.

Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. 11. Effects of pH, competitive inhibition, and chromium(III) modification on the reaction of plastocyanin with cytochrome f

S. Chapman, A. Sykes, C. Knox, 1985 .

Isolation and characterization of the cytochrome domain of flavocytochrome b2 expressed independently in Escherichia coli.

G. Moore, S. Chapman, G. Reid, 1992, The Biochemical journal.

Multi-heme cytochromes--new structures, new chemistry.

S. Chapman, C. Mowat, 2005, Dalton transactions.

An octaheme c‐type cytochrome from Shewanella oneidensis can reduce nitrite and hydroxylamine

S. Chapman, Sally J. Atkinson, G. Reid, 2007, FEBS letters.

Substitution of a haem-iron axial ligand in flavocytochrome b2.

S. Chapman, F. Manson, G. Reid, 1993, Biochimica et biophysica acta.

NMR redox studies of flavocytochrome c3 from Shewanella frigidimarina

S. Chapman, D. Turner, A. V. Xavier, 2003 .

Modulation of flavocytochrome b2 intraprotein electron transfer via an interdomain hinge region.

S. Chapman, G. Reid, R. Sharp, 1996, The Biochemical journal.

Electrochemistry of the flavodehydrogenase domain of flavocytochrome b2 engineered for l-mandelate dehydrogenase activity

S. Chapman, H. Hill, Huihong Liu, 2001 .

The role of Thr268 and Phe393 in cytochrome P450 BM3.

Jonathan P. Clark, M. Walkinshaw, S. Daff, 2006, Journal of inorganic biochemistry.

4-Cyanopyridine, a Versatile Spectroscopic Probe for Cytochrome P450 BM3*

Jonathan P. Clark, T. Ost, S. Daff, 2004, Journal of Biological Chemistry.

Changing the heme ligation in flavocytochrome b2: substitution of histidine-66 by cysteine

A. Munro, S. Chapman, L. Quaroni, 2000, JBIC Journal of Biological Inorganic Chemistry.

Determination of the orientation of the axial ligands and of the magnetic properties of the haems in the tetrahaem ferricytochrome from Shewanella frigidimarina

S. Chapman, R. Louro, D. Turner, 2002, FEBS letters.

L-mandelate dehydrogenase from Rhodotorula graminis: comparisons with the L-lactate dehydrogenase (flavocytochrome b2) from Saccharomyces cerevisiae.

S. Chapman, C. A. Fewson, G. Reid, 1993, The Biochemical journal.

Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P-450 BM3.

G. Chumanov, A. Munro, M. Noble, 1998, Biochemistry.

Isolation and partial characterization of an extradiol non-haem iron dioxygenase which preferentially cleaves 3-methylcatechol.

S. Chapman, M. Wallis, 1990, The Biochemical journal.

Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.

T. Ost, P. Taylor, M. Walkinshaw, 2001, Biochemistry.

Control of electron transfer in neuronal NO synthase.

A. Munro, M. Noble, S. Daff, 2001, Biochemical Society transactions.

Catalytically functional flavocytochrome chimeras of P450 BM3 and nitric oxide synthase.

A. Munro, M. Noble, S. Chapman, 2002, Journal of inorganic biochemistry.

The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella.

S. Chapman, G. Reid, C. Schwalb, 2001, Biochemical Society transactions.

Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins. Part 10. The assignment of binding sites in the reactions of plastocyanin (and azurin) with non-physiological protein redox partners

S. Chapman, A. Sykes, C. Knox, 1984 .

Kinetic studies on 1 : 1 electron-transfer reactions involving blue copper proteins. Part 7. Effects of pH and redox-inactive [Pt(NH3)6]4+ on reactions of parsley plastocyanin with different inorganic redox partners

S. Chapman, I. Sanemasa, A. Sykes, 1983 .

KINETIC STUDIES OF 1:1 ELECTRON-TRANSFER REACTIONS INVOLVING BLUE COPPER PROTEINS. PART 10. THE ASSIGNMENT OF BINDING SITES IN THE REACTIONS OF PLASTOCYANIN (AND AZURIN) WITH NONPHYSIOLOGICAL PROTEIN REDOX PARTNERS

S. Chapman, A. Sykes, C. Knox, 1985 .

KINETIC STUDIES ON 1:1 ELECTRON-TRANSFER REACTIONS INVOLVING BLUE COPPER PROTEINS. PART 7. EFFECTS OF PH AND REDOX-INACTIVE HEXAAMMINEPLATINUM(4+) ON REACTIONS OF PARSLEY PLASTOCYANIN WITH DIFFERENT INORGANIC REDOX PARTNERS

S. Chapman, I. Sanemasa, A. Sykes, 1984 .

Expression, purification and characterization of cytochrome P450 Biol: a novel P450 involved in biotin synthesis in Bacillus subtilis

A. Munro, S. Chapman, L. Quaroni, 2001, JBIC Journal of Biological Inorganic Chemistry.

The solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel family structural motif.

S. Chapman, D. Turner, L. Brennan, 2008, Biochemistry.

New insights into the catalytic cycle of flavocytochrome b2.

S. Daff, S. Chapman, G. Reid, 1996, Biochemistry.

Flavins and flavoproteins 2002

N. Scrutton, S. Chapman, R. Perham, 2002 .

A new method for extraction of iron-molybdenum cofactor (FeMoco) from nitrogenase adsorbed to DEAE-cellulose. 1. Effects of anions, cations, and preextraction treatments.

D. Wink, S. Chapman, A. Hickman, 1989, Biochemistry.

Expression, purification and characterisation of a Bacillus subtilis ferredoxin: a potential electron transfer donor to cytochrome P450 BioI.

A. Munro, S. Chapman, C. von Wachenfeldt, 2003, Journal of inorganic biochemistry.

Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase

N. C. Price, R. Baxter, A. Munro, 2000 .

Edinburgh Research Explorer Exploring the Mechanism of Tryptophan 2,3-dioxygenase Exploring the Mechanism of Tryptophan 2,3-dioxygenase

Sarah J. Thackray, S. Chapman, C. Mowat, 2022 .

Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase

Sarah J. Thackray, G. Montelione, T. Acton, 2007, Proceedings of the National Academy of Sciences.

The solution structure of a tetraheme cytochrome from Shewanella frigidimarina reveals a novel family structural motif.

S. Chapman, D. Turner, L. Brennan, 2008, Biochemistry.

Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria. [Erratum to document cited in CA117(25):247691n]

S. Chapman, S. L. Pealing, A. Black, 1993 .

Concerning the binding site on plastocyanin for its natural redox partner cytochrome f

S. Chapman, A. Sykes, C. Knox, 1983 .