Accessibility of the Distal Heme Face, Rather than Fe−His Bond Strength, Determines the Heme-Nitrosyl Coordination Number of Cytochromes c‘: Evidence from Spectroscopic Studies-Reference-Cited by-同舟云学术

Accessibility of the Distal Heme Face, Rather than Fe−His Bond Strength, Determines the Heme-Nitrosyl Coordination Number of Cytochromes c‘: Evidence from Spectroscopic Studies

Published:2005-05-26 Issue:24 Volume:44 Page:8664-8672
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Andrew Colin R.¹,Kemper Lenord J.¹,Busche Tammy L.¹,Tiwari Arianne M.¹,Kecskes Michael C.¹,Stafford James M.¹,Croft Lea C.¹,Lu Shen¹,Moënne-Loccoz Pierre¹,Huston Willa¹,Moir James W. B.¹,Eady Robert R.¹

Affiliation:

1. Department of Chemistry & Biochemistry, Eastern Oregon University, La Grande, Oregon 97850, Department of Environmental & Biomolecular Systems, OGI School of Science & Engineering, Oregon Health & Science University, Beaverton, Oregon 97006, Department of Biology, University of York, U.K., and Department of Biological Chemistry, John Innes Centre, Norwich, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi050428g

Reference59 articles.

1. Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NOx Redox Chemistry

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