How Do Heme-Protein Sensors Exclude Oxygen? Lessons Learned from Cytochrome c′,Nostoc puntiformeHeme Nitric Oxide/Oxygen-Binding Domain, and Soluble Guanylyl Cyclase-Reference-Cited by-同舟云学术

How Do Heme-Protein Sensors Exclude Oxygen? Lessons Learned from Cytochrome c′,Nostoc puntiformeHeme Nitric Oxide/Oxygen-Binding Domain, and Soluble Guanylyl Cyclase

Published:2012-11 Issue:9 Volume:17 Page:1246-1263
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Tsai Ah-lim¹,Martin Emil²,Berka Vladimir¹,Olson John S.³

Affiliation:

1. Division of Hematology, University of Texas Health Science Center at Houston, Houston, Texas.

2. Division of Cardiology, Department of Internal Medicine, University of Texas Health Science Center at Houston, Houston, Texas.

3. Department of Biochemistry and Cell Biology and W.M. Keck Center for Computational Biology, Rice University, Houston, Texas.

Publisher

Mary Ann Liebert Inc

Subject

Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry,Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry

Link

http://www.liebertpub.com/doi/pdf/10.1089/ars.2012.4564

Reference132 articles.

1. O2-specific regulation of the ferrous heme-based sensor kinase FixL from Sinorhizobium meliloti and its aberrant inactivation in the ferric form

2. Six- to Five-Coordinate Heme−Nitrosyl Conversion in Cytochrome c‘ and Its Relevance to Guanylate Cyclase

3. Resonance Raman Studies of Cytochrome c‘ Support the Binding of NO and CO to Opposite Sides of the Heme: Implications for Ligand Discrimination in Heme-Based Sensors

4. 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

5. A Novel Kinetic Trap for NO Release from Cytochrome c‘: A Possible Mechanism for NO Release from Activated Soluble Guanylate Cyclase

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