Heme Axial Methionine Fluxionality in Hydrogenobacter Thermophilus Cytochrome C552

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2004 May 27

PMID 15161973

Citations 24

Authors

Linghao Zhong

Xin Wen

Terry M Rabinowitz

Brandy S Russell

Elizabeth F Karan

Kara L Bren

Affiliations

Soon will be listed here.

Abstract

The heme group in paramagnetic (S = 1/2) ferricytochromes c typically displays a markedly asymmetric distribution of unpaired electron spin density among the heme pyrrole beta substituents. This asymmetry is determined by the orientations of the heme axial ligands, histidine and methionine. One exception to this is ferricytochrome c(552) from Hydrogenobacter thermophilus, which has similar amounts of unpaired electron spin density at the beta substituents on all four heme pyrroles. Here, determination of the orientation of the magnetic axes and analysis of NMR line shapes for H. thermophilus ferricytochrome c(552) is performed. These data reveal that the unusual electronic structure for this protein is a result of fluxionality of the heme axial methionine. It is proposed that the ligand undergoes inversion at the pyramidal sulfur, and the rapid interconversion between two diastereomeric forms results in the unusual heme electronic structure. Thus a fluxional process for a metal-bound amino acid side chain has now been identified.

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