An Intermediate Conformational State during Ligand Binding to Cytochrome c Oxidase Detected by Time-resolved Resonance Raman Analyses of Heme Peripheral Groups

2012 ◽  
Vol 41 (2) ◽  
pp. 178-180 ◽  
Author(s):  
Izumi Ishigami ◽  
Takeshi Nishigaki ◽  
Kyoko Shinzawa-Itoh ◽  
Shinya Yoshikawa ◽  
Satoru Nakashima ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Ligand Binding ◽  
Cytochrome C Oxidase ◽  
Resonance Raman ◽  
Conformational State ◽  
Time Resolved

scholarly journals Time-resolved infrared studies of the dynamics of ligand binding to cytochrome c oxidase

1991 ◽  
Author(s):  
R. B. Dyer ◽  
Kristen A. Peterson ◽  
Page O. Stoutland ◽  
Oloef Einarsdottir ◽  
William H. Woodruff
Keyword(s):  
Cytochrome C ◽  
Ligand Binding ◽  
Cytochrome C Oxidase ◽  
Time Resolved ◽  
Infrared Studies

scholarly journals Time-Resolved Resonance Raman Study of Dioxygen Reduction by Cytochrome c Oxidase

1998 ◽  
pp. 57-71
Author(s):  
Teizo Kitagawa ◽  
Takashi Ogura ◽  
Shun Hirota ◽  
Denis A. Proshlyakov ◽  
Jorg Matysik ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Resonance Raman ◽  
Time Resolved ◽  
Dioxygen Reduction ◽  
Raman Study

Mechanism of Dioxygen Reduction by Cytochrome c Oxidase as Studied by Time-Resolved Resonance Raman Spectroscopy

1998 ◽  
pp. 102-105
Author(s):  
Takashi Ogura ◽  
Denis A. Proshlyakov ◽  
Jörg Matysik ◽  
Evan H. Appelman ◽  
Kyoko Shinzawa-Itoh ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Time Resolved ◽  
Dioxygen Reduction

Time-resolved resonance Raman elucidation of the pathway for dioxygen reduction by cytochrome c oxidase

1993 ◽  
Vol 115 (19) ◽  
pp. 8527-8536 ◽  
Author(s):  
Takashi Ogura ◽  
Satoshi Takahashi ◽  
Shun Hirota ◽  
Kyoko Shinzawa-Itoh ◽  
Shinya Yoshikawa ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Resonance Raman ◽  
Time Resolved ◽  
Dioxygen Reduction

Resonance Raman spectroscopy of the cytochrome c oxidase from Paracoccus denitrificans

Biochemistry ◽  
1993 ◽  
Vol 32 (27) ◽  
pp. 6923-6927 ◽  
Author(s):  
Stephen R. Lynch ◽  
Richard H. Carter ◽  
Robert A. Copeland
Keyword(s):  
Raman Spectroscopy ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Paracoccus Denitrificans ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman

scholarly journals 3P102 Resonance Raman Spectra of Cytochrome c Oxidase Reconstituted in Phospholipid Vesicles

2005 ◽  
Vol 45 (supplement) ◽  
pp. S229
Author(s):  
M. Yamada ◽  
S. Yamaguchi ◽  
T. Ogura ◽  
S. Yoshikawa
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Raman Spectra ◽  
Resonance Raman ◽  
Phospholipid Vesicles ◽  
Resonance Raman Spectra

scholarly journals Probing the Proton-Loading Site of Cytochrome C Oxidase Using Time-Resolved Fourier Transform Infrared Spectroscopy

Molecules ◽  
2020 ◽  
Vol 25 (15) ◽  
pp. 3393
Author(s):  
Elena Gorbikova ◽  
Sergey A. Samsonov ◽  
Ruslan Kalendar
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Fourier Transform Infrared Spectroscopy ◽  
Paracoccus Denitrificans ◽  
Fourier Transform Infrared ◽  
Double Difference ◽  
Time Resolved ◽  
Fast Kinetic

Crystal structure analyses at atomic resolution and FTIR spectroscopic studies of cytochrome c oxidase have yet not revealed protonation or deprotonation of key sites of proton transfer in a time-resolved mode. Here, a sensitive technique to detect protolytic transitions is employed. In this work, probing a proton-loading site of cytochrome c oxidase from Paracoccus denitrificans with time-resolved Fourier transform infrared spectroscopy is presented for the first time. For this purpose, variants with single-site mutations of N131V, D124N, and E278Q, the key residues in the D-channel, were studied. The reaction of mutated CcO enzymes with oxygen was monitored and analyzed. Seven infrared bands in the “fast” kinetic spectra were found based on the following three requirements: (1) they are present in the “fast” phases of N131V and D124N mutants, (2) they have reciprocal counterparts in the “slow” kinetic spectra in these mutants, and (3) they are absent in “fast” kinetic spectra of the E278Q mutant. Moreover, the double-difference spectra between the first two mutants and E278Q revealed more IR bands that may belong to the proton-loading site protolytic transitions. From these results, it is assumed that several polar residues and/or water molecule cluster(s) share a proton as a proton-loading site. This site can be propionate itself (holding only a fraction of H+), His403, and/or water cluster(s).

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