Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: Characterization and their catalytic activities-Reference-Cited by-同舟云学术

Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: Characterization and their catalytic activities

Published:1991-10 Issue:1 Volume:180 Page:138-144
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Adachi Shin-ichi,Nagano Shingo,Watanabe Yoshihito,Ishimori Koichiro,Morishima Isao

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference27 articles.

1. The crystal structure of cytochrome c peroxidase.

2. Structure of beef liver catalase

3. The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.

4. Cytochrome P-450 and chloroperoxidase: thiolate-ligated heme enzymes. Spectroscopic determination of their active-site structures and mechanistic implications of thiolate ligation

5. Magnetic circular dichroism studies. 43. Oxidized cytochrome P-450. Magnetic circular dichroism evidence for thiolate ligation in the substrate-bound form. Implications for the catalytic mechanism

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