Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/6683
Title: O2 activation in cytochrome oxidase and in other heme proteins
Authors: Babcock, Gerald
Zhang, Yong
Varotsis, Constantinos 
Keywords: Cytochrome oxidase
Hemoproteins
Oxygen
Metabolism
Enzymes
Issue Date: 1992
Publisher: Elsevier
Source: Biochimica et biophysica acta - bioenergetics, 1992, Volume 1101, Issue 2, Pages 192-194
Abstract: In applying room-temperature, time-resolved optical and resonance-Raman spectroscopies to the cytochrome oxidase/dioxygen reaction, we have been fortunate in being able to detect intermediates in this process both before and after the O-O bond scission reaction occurs (e.g., Refs. 1-9). This behavior contrasts markedly with the situation in the cytochromes P-450 (P450), for example, where the structure of key intermediates, subsequent to the initial oxy complex [10], in the bond cleavage and substrate hydroxylating reactions have been inferred from model studies, chemical reasoning, and genetic modification, but have not been detected directly
URI: http://ktisis.cut.ac.cy/handle/10488/6683
ISSN: 0005-2728
DOI: 10.1016/0005-2728(92)90222-N
Rights: © 1992 Elsevier Science Publishers B.V. All rights reserved
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