Active Site Structure in Cytochrome c Peroxidase and Myoglobin Mutants: Effects of Altered Hydrogen Bonding to the Proximal Histidine-Reference-Cited by-同舟云学术

Active Site Structure in Cytochrome c Peroxidase and Myoglobin Mutants: Effects of Altered Hydrogen Bonding to the Proximal Histidine

Published:1996-01-01 Issue:47 Volume:35 Page:15120-15128
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sinclair R.¹,Hallam S.¹,Chen M.¹,Chance B.¹,Powers L.¹

Affiliation:

1. National Center for the Design of Molecular Function, Utah State University, Logan, Utah 84322-4630, and Department of Biochemistry and Biophysics, University of Pennsylvania Medical School, Philadelphia, Pennsylvania 19104

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi961064i

Reference73 articles.

1. Movement of Fe with respect to the heme plane in the R-T transition of carp hemoglobin. An extended x-ray absorption fine structure study.

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