Biphasic recombination of photodissociated CO compound of cytochrome o(s) from Vitreoscilla.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference9 articles.
1. The binding of cyanide and carbon monoxide to cytochrome o purified from Vitreoscilla. Evidence for subunit interaction in the reduced protein.
2. Formation and decay of the primary oxygen compound of cytochrome oxidase at room temperature as observed by stopped flow, laser flash photolysis and rapid scanning.
3. Spectral evidence for the existence of a second cytochrome o in whole cells of Vitreoscilla.
4. Oxidases and Related Redox Systems;Orii,1982
5. Biochemical and Clinical Aspects of Hemoglobin Abnormalities;Pennelly,1978
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Site-Directed Mutagenesis of Bacterial Hemoglobin: The Role of Glutamine (E7) in Oxygen-Binding in the Distal Heme Pocket;Archives of Biochemistry and Biophysics;1998-01
2. Nonvertebrate hemoglobins: Structural bases for reactivity;Progress in Biophysics and Molecular Biology;1997
3. Transcriptional Control of Vitreoscilla Hemoglobin Synthesis;Structure and Function of Invertebrate Oxygen Carriers;1991
4. Photodissociation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation.;Journal of Biological Chemistry;1986-03
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