Equilibrium and Transient State Spectrophotometric Studies of the Mechanism of Reduction of the Flavoprotein Domain of P450BM-3-Reference-Cited by-同舟云学术

Equilibrium and Transient State Spectrophotometric Studies of the Mechanism of Reduction of the Flavoprotein Domain of P450BM-3

Published:1996-01-01 Issue:22 Volume:35 Page:7058-7068
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sevrioukova Irina¹,Shaffer Catherine¹,Ballou David P.¹,Peterson Julian A.¹

Affiliation:

1. Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235-9038, and Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109-0606

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi960060a

Reference57 articles.

1. The haemoglobin-like protein (HMP) ofEscherichia colihas ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+reductases

2. The effect of NADPH concentration on the reduction of cytochrome P-450 LM2.

3. Bevington, P. R. (1969) inData reduction & error analysis for the physical sciences, pp 235−242, McGraw-Hill, New York.

4. Fatty acid monooxygenation by cytochrome P-450BM-3.

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