Format

Send to

Choose Destination
Biophys J. 1998 Jun;74(6):3241-9.

Fatty acid-induced alteration of the porphyrin macrocycle of cytochrome P450 BM3.

Author information

1
Department of Pure and Applied Chemistry, University of Strathclyde, Glasgow, Scotland.

Abstract

Surface-enhanced resonance Raman scattering (SERRS) of substrate-free and substrate-bound forms of the P450 domain of cytochrome P450 BM3 are reported and assigned. Substrate-free P450 yields mixed spin heme species in which the pentacoordinate high-spin arrangement is dominant. The addition of laurate or palmitate leads to an increase in high spin content and to an allosteric activation of heme mode v29, which is sensitive to peripheral heme/protein interactions. Differences between laurate and palmitate binding are observed in the relative intensities of a number of bands and the splitting of the heme vinyl modes. Laurate binding to P450 results in different protein environments being experienced by each vinyl mode, whereas palmitate binding produces a smaller difference. The results demonstrate the ability of SERRS to probe substrate/prosthetic group interactions within an active site, at low protein concentrations.

PMID:
9635777
PMCID:
PMC1299664
DOI:
10.1016/S0006-3495(98)78030-0
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center