Cytochrome P450cam: SS- dimer and -SH derivative reactivities

J. D. Lipscomb; J. E. Harrison; K. M. Dus; I. C. Gunsalus

doi:10.1016/0006-291X(78)91461-4

Cytochrome P450_cam: SS- dimer and -SH derivative reactivities

J. D. Lipscomb, J. E. Harrison, K. M. Dus, I. C. Gunsalus

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

N-ethyl-maleimide alkylation converts ferric P450_cam to a (succinimido-cys)₄ protein with native optical and EPR spectra but insensitive to substrate induced shift of iron to high spin with Soret absorption to higher energy and inactive in putidaredoxin ferric-ferrous reduction. On photo or chemical reduction the ferrous protein oxygenates and, with reduced putidaredoxin, converts substrate to product. Mild oxidation of P450_cam yields a disulfide dimer whose properties on alkylation of 3 sulfhydryls equal the succinimido₄ monomer; additional alkylation converts either monomer or dimer to a P420.

Original language	English (US)
Pages (from-to)	771-778
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	83
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(78)91461-4
State	Published - Aug 14 1978
Externally published	Yes

Bibliographical note

Funding Information:
Supported in part by HEW PHS Grants GM 21161 and AM 00562. We are indebted to Dr. B. S. Shastry for checking the cysteinyl and succinimido-cysteine content of the NEM treated cyt m.

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title = "Cytochrome P450cam: SS- dimer and -SH derivative reactivities",

abstract = "N-ethyl-maleimide alkylation converts ferric P450cam to a (succinimido-cys)4 protein with native optical and EPR spectra but insensitive to substrate induced shift of iron to high spin with Soret absorption to higher energy and inactive in putidaredoxin ferric-ferrous reduction. On photo or chemical reduction the ferrous protein oxygenates and, with reduced putidaredoxin, converts substrate to product. Mild oxidation of P450cam yields a disulfide dimer whose properties on alkylation of 3 sulfhydryls equal the succinimido4 monomer; additional alkylation converts either monomer or dimer to a P420.",

author = "Lipscomb, {J. D.} and Harrison, {J. E.} and Dus, {K. M.} and Gunsalus, {I. C.}",

note = "Funding Information: Supported in part by HEW PHS Grants GM 21161 and AM 00562. We are indebted to Dr. B. S. Shastry for checking the cysteinyl and succinimido-cysteine content of the NEM treated cyt m.",

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T2 - SS- dimer and -SH derivative reactivities

AU - Lipscomb, J. D.

AU - Harrison, J. E.

AU - Dus, K. M.

AU - Gunsalus, I. C.

N1 - Funding Information: Supported in part by HEW PHS Grants GM 21161 and AM 00562. We are indebted to Dr. B. S. Shastry for checking the cysteinyl and succinimido-cysteine content of the NEM treated cyt m.

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AB - N-ethyl-maleimide alkylation converts ferric P450cam to a (succinimido-cys)4 protein with native optical and EPR spectra but insensitive to substrate induced shift of iron to high spin with Soret absorption to higher energy and inactive in putidaredoxin ferric-ferrous reduction. On photo or chemical reduction the ferrous protein oxygenates and, with reduced putidaredoxin, converts substrate to product. Mild oxidation of P450cam yields a disulfide dimer whose properties on alkylation of 3 sulfhydryls equal the succinimido4 monomer; additional alkylation converts either monomer or dimer to a P420.

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