NDLI: Electron transfer reactions in biological systems: the reduction of ferricytochrome c by chromous ions.

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Electron transfer reactions in biological systems: the reduction of ferricytochrome c by chromous ions.

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Electron transfer reactions in biological systems: the reduction of ferricytochrome c by chromous ions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Grimes, C. J. Fleischer, E. B. Piszkiewicz, D.
Abstract	Chromous ion reacts with ferricytochrome c to yield a one-to-one Cr(III)-ferrocytochrome c complex. This material, when hydrolyzed by trypsin and subjected to chromatographic procedures, yielded two fragments containing chromium. The amino-acid compositions and chemical characteristics of each of these fragments indicated that the chromium had crosslinked two segments of polypeptide chain; these were residues 40-53-Cr(III)-residues 61-72 and residues 40-53-Cr(III)-residues 61-73. Examination of a model of the ferricytochrome c molecule indicated that only two residues of the crosslinked peptides were sufficiently close to allow crosslinking to take place. These residues were tyrosine 67 and asparagine 52. Enzymatic hydrolysis of one of those fragments by aminopeptidase M supported this identification. The position of the chromic ion implies what is the path of electron transfer from the chromous ion to the ferric ion in this chemical reduction of cytochrome c, and suggests a possible path of electron transfer in biological oxidation-reduction reactions.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	71
Language	English
Publisher	National Academy of Sciences
Publisher Date	1974-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chromium Metabolism Cytochrome c Group Amino Acid Sequence Aminopeptidases Animals Asparagine Autoradiography Chromatography, Gel Chromium Radioisotopes Electron Transport Horses Hydrolysis In Vitro Techniques Myocardium Enzymology Oxidation-Reduction Peptides Protein Binding Protein Conformation Structure-Activity Relationship Trypsin Tyrosine Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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