Cobalt-substituted cytochrome P-450cam.

G. C. Wagner*, I. C. Gunsalus, M. Y. Wang, B. M. Hoffman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

Reconstitution of the apo-cytochrome with cobalt protoporphyrin provides a faithful P-450cam analogue as characterized by optical, ligand-binding, and enzymatic parameters. The thiol and cyanide complexes exhibit Soret "hyper" spectra, not previously observed in cobalt porphyrins. Substrate-induced spectral changes and limited stereospecific hydroxylation activity are retained in the cobalt P-450cam. The EPR (electron paramagnetic resonance) spectra of the reduced cobaltous protein indicate clearly an endogenous axial ligand other than a nitrogenous base and support an assignment of thiolate coordination. A thiolate ligand is also indicated by EPR measurements in the oxygenated cobaltous analogue. By analogy, these studies suggest that the native ferrous and oxygenated P-450cam states retain a thiolate axial ligand.

Original languageEnglish (US)
Pages (from-to)6266-6273
Number of pages8
JournalJournal of Biological Chemistry
Volume256
Issue number12
StatePublished - Jun 25 1981

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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