Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as-isolated" enzyme and characterization of the cyanide adduct-Reference-Cited by-同舟云学术

Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as-isolated" enzyme and characterization of the cyanide adduct

Published:1995-09-26 Issue:38 Volume:34 Page:12144-12151
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sun Jie,Osborne Jeffrey P.,Kahlow Michael A.,Kaysser Tamma M.,Gennis Robert B.,Loehr Thomas M.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00038a007

Reference75 articles.

1. Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase

2. Sulfmyoglobin. Resonance Raman spectroscopic evidence for an iron-chlorin prosthetic group.

3. Resonance Raman spectroscopy of metallochlorins: models for green heme protein prosthetic groups

4. Facile lactonization and inversion of vicinal diols in heme d-type chlorins: a spectroscopic study

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