Investigation of the Low Frequency Dynamics of Heme Proteins: Native and Mutant Cytochrome P450cam and Redox Partner Complexes-Reference-Cited by-同舟云学术

Investigation of the Low Frequency Dynamics of Heme Proteins: Native and Mutant Cytochrome P450cam and Redox Partner Complexes

Published:2011-03-10 Issue:18 Volume:115 Page:5665-5677
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Karunakaran Venugopal¹,Denisov Ilia²,Sligar Stephen G.²,Champion Paul M.¹

Affiliation:

1. Department of Physics and Center for Interdisciplinary Research on Complex Systems, Northeastern University, Boston, Massachusetts 02115, United States

2. Department of Biochemistry, University of Illinois, Urbana, Illinois 61801, United States

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp112298y

Reference79 articles.

1. Structure and Chemistry of Cytochrome P450

2. Resonance Raman detection of an iron-sulfur bond in cytochrome P 450cam

3. Sulfur donor ligand binding to ferric cytochrome P-450-CAM and myoglobin. Ultraviolet-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic investigation of the complexes.

4. Role of Arg112 of Cytochrome P450cam in the Electron Transfer from Reduced Putidaredoxin

5. A structure-based model for cytochrome P450cam-putidaredoxin interactions

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