S. Sligar

发表

Role of NADPH:cytochrome c reductase and DT-diaphorase in the biotransformation of mitomycin C1.

S. Keyes, P. Fracasso, D. Heimbrook, 1984, Cancer research.

Engineering and design of blood substitutes.

K. E. Sanders, S. Sligar, G. Ackers, 1996, Current opinion in structural biology.

A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase.

S. Sligar, I. C. Gunsalus, 1976, Proceedings of the National Academy of Sciences of the United States of America.

Epoxidation of olefins by hydroperoxo-ferric cytochrome P450.

S. Sligar, J. Dawson, Shengxi Jin, 2003, Journal of the American Chemical Society.

Metabolic activation of mitomycin C by liver microsomes and nuclei.

S. Sligar, A. Sartorelli, K. A. Kennedy, 1982, Biochemical pharmacology.

A Pathfinder in High-Pressure Bioscience: In Memoriam of Gaston Hui Bon Hoa

G. Petsko, S. Sligar, J. Kornblatt, 2021, Biology.

Superoxide anion production by the autoxidation of cytochrome P450cam.

S. Sligar, S. Sligar, J. Lipscomb, 1974, Biochemical and biophysical research communications.

Letter: Origin of the anomalous Soret spectra of carboxycytochrome P-450.

C. R. Connell, L. K. Hanson, W. Eaton, 1976, Journal of the American Chemical Society.

The Chemical Basis of Mixed Function Oxidation

S. Sligar, D. Pearson, 1982 .

Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam.

S. Sligar, J. Lipscomb, I. C. Gunsalus, 1976, The Journal of biological chemistry.

CHAPTER 16 – Pseudomonas Cytochromes P-450

S. Sligar, I. C. Gunsalus, B. Unger, 1986 .

Oxygenase-catalyzed biological hydroxylations.

S. Sligar, I. C. Gunsalus, T. Pederson, 1975, Annual review of biochemistry.

The status of high-valent metal oxo complexes in the P450 cytochromes.

I. Schlichting, Konstanze von Koenig, S. Sligar, 2006, Journal of inorganic biochemistry.

Engineering and design.

Gregory A. Petsko, Stephen G. Sligar, G. Petsko, 1995, Current opinion in structural biology.

The catalytic pathway of cytochrome p450cam at atomic resolution.

J Berendzen, R M Sweet, D. E. Benson, 2000, Science.

Development of broad-host-range vectors for expression of cloned genes in Pseudomonas.

S. Sligar, M. Schuler, J. Werneke, 1985, Gene.

Diversities and Similarities in P450 Systems: An Introduction

S. Sligar, M. Schuler, 2007 .

Structure and chemistry of cytochrome P450.

Ilme Schlichting, I. Schlichting, S. Sligar, 2005, Chemical reviews.

Hyperfine structure of the hydrogen atom in CaF2 as a function of temperature

S. Sligar, H. Blum, 1971 .

Engineering and designProtein engineering for molecular electronics

F. Salemme, S. Sligar, 1992 .

Protein engineering for molecular electronics

F. Salemme, S. Sligar, 1992, Current Biology.

Oxygen reduction by the P450 monoxygenase systems.

S. Sligar, I. C. Gunsalus, 1978, Advances in enzymology and related areas of molecular biology.

Chemotherapeutic attack of hypoxic tumor cells by the bioreductive alkylating agent mitomycin C.

S. Keyes, P. Fracasso, D. Heimbrook, 1985, Advances in enzyme regulation.

Redox regulation of cytochrome P450cam mixed function oxidation by putidaredoxin and camphor ligation.

S. Sligar, I. C. Gunsalus, 1976, Biochimie.

Coupling of spin, substrate, and redox equilibria in cytochrome P450.

S. Sligar, S G Sligar, 1976, Biochemistry.

Solution structure of apocytochrome b562

A. Joshua Wand, A. Wand, S. Sligar, 1994, Nature Structural Biology.

A retinoic acid binding cytochrome P450: CYP120A1 from Synechocystis sp. PCC 6803.

Na Ke, Jerome Baudry, J. Baudry, 2005, Archives of biochemistry and biophysics.

Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli.

S. Sligar, I. C. Gunsalus, B. Unger, 1986, The Journal of biological chemistry.

Crystal structures of substrate-free and retinoic acid-bound cyanobacterial cytochrome P450 CYP120A1.

Ilme Schlichting, Na Ke, I. Schlichting, 2008, Biochemistry.

Sensitizer-linked substrates and ligands: ruthenium probes of cytochrome P450 structure and mechanism.

H. Gray, A. Dunn, Michael T. Green, 2002, Methods in enzymology.

Proton coupling in the cytochrome P-450 spin and redox equilibria.

S. Sligar, I. C. Gunsalus, 1979, Biochemistry.

Engineering protein orientation at surfaces to control macromolecular recognition events.

S. Sligar, P. Stayton, M. McLean, 1993, Analytical chemistry.

The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM.

S. Sligar, J. Dawson, M. Sono, 2005, Archives of biochemistry and biophysics.

EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: Mutation-induced changes in the proton delivery system [15]

S. Sligar, B. Hoffman, Roman Davydov, 1999 .

A role of the putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations.

S. Sligar, S. Sligar, J. Lipscomb, 1974, Proceedings of the National Academy of Sciences of the United States of America.

Equilibrium states and dynamic reactions of iron in the camphor monoxygenase system.

S. Sligar, I. C. Gunsalus, 1976, Advances in Experimental Medicine and Biology.

Molecular recognition mediated by bound water. A mechanism for star activity of the restriction endonuclease EcoRI.

S. Sligar, S. Sligar, C. R. Robinson, 1993, Journal of molecular biology.

Cloning and expression of a member of a new cytochrome P-450 family: cytochrome P-450lin (CYP111) from Pseudomonas incognita

S. Sligar, S. Sligar, J. D. Ropp, 1993, Journal of bacteriology.

Hydrostatic and osmotic pressure as tools to study macromolecular recognition.

S. Sligar, S. Sligar, C R Robinson, 1995, Methods in enzymology.

Changes in solvation during DNA binding and cleavage are critical to altered specificity of the EcoRI endonuclease.

S. Sligar, S. Sligar, C R Robinson, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Experiences in biochemical perception

S. Sligar, I. C. Gunsalus, L. Ornston, 1982 .

Substrate interaction with cytochrome P-450.

S. Sligar, D. L. Cinti, S. Sligar, 1981, Pharmacology & therapeutics.