Cytochrome P450cam: SS- dimer and -SH derivative reactivities

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

Research output: Contribution to journalArticle

18 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)771-778
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume83
Issue number3
DOIs
StatePublished - Aug 14 1978
Externally publishedYes

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Camphor 5-Monooxygenase
Alkylation
Cytochromes
Dimers
Derivatives
Monomers
Substrates
Disulfides
Paramagnetic resonance
Proteins
Iron
Oxidation
putidaredoxin

Cite this

Cytochrome P450cam : SS- dimer and -SH derivative reactivities. / Lipscomb, John D; Harrison, J. E.; Dus, K. M.; Gunsalus, I. C.

In: Biochemical and Biophysical Research Communications, Vol. 83, No. 3, 14.08.1978, p. 771-778.

Research output: Contribution to journalArticle

Lipscomb, John D ; Harrison, J. E. ; Dus, K. M. ; Gunsalus, I. C. / Cytochrome P450cam : SS- dimer and -SH derivative reactivities. In: Biochemical and Biophysical Research Communications. 1978 ; Vol. 83, No. 3. pp. 771-778.
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