IR signatures of the metal centres of bovine cytochrome c oxidase: assignments and redox-linkage

2013 ◽  
Vol 41 (5) ◽  
pp. 1242-1248 ◽  
Author(s):  
Raksha Dodia ◽  
Amandine Maréchal ◽  
Simona Bettini ◽  
Masayo Iwaki ◽  
Peter R. Rich
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Redox Cycling ◽  
Difference Spectra ◽  
Redox States ◽  
Ir Bands ◽  
Specific Metal

Assignments of IR bands of reduced minus oxidized IR difference spectra of bovine and related cytochrome c oxidases are reviewed and their linkages to specific metal centres are assessed. To aid this, redox-poised difference spectra in the presence of cyanide or carbon monoxide are presented. These ligands fix the redox states of either haem a3 alone or haem a3 and CuB respectively, while allowing redox cycling of the remaining centres.

scholarly journals S11.25 X-ray structure of carbon monoxide at copper site of the dinuclear site of cytochrome c oxidase

2008 ◽  
Vol 1777 ◽  
pp. S71
Author(s):  
Kazumasa Muramoto ◽  
Naoki Nakagawa ◽  
Maki Taniguchi ◽  
Katsumasa Kanda ◽  
Kyoko Shinzawa-Itoh ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
X Ray ◽  
Copper Site

Carbon Monoxide Specifically Inhibits Cytochrome C Oxidase of Human Mitochondrial Respiratory Chain

2003 ◽  
Vol 93 (3) ◽  
pp. 142-146 ◽  
Author(s):  
Jose-Ramon Alonso ◽  
Francesc Cardellach ◽  
Sònia López ◽  
Jordi Casademont ◽  
Òscar Miró
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Mitochondrial Respiratory

scholarly journals Proton linkage of cytochrome a oxidoreduction in carbon monoxide-treated cytochrome c oxidase

1999 ◽  
Vol 1412 (2) ◽  
pp. 184-189 ◽  
Author(s):  
Michael I Verkhovsky ◽  
Nikolai Belevich ◽  
Joel E Morgan ◽  
Mårten Wikström
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase

Temperature dependence of the reduction potential in CuA in carbon monoxide-inhibited cytochrome c oxidase

Biochemistry ◽  
1986 ◽  
Vol 25 (1) ◽  
pp. 167-171 ◽  
Author(s):  
Hsin Wang ◽  
David F. Blair ◽  
Walther R. Ellis ◽  
Harry B. Gray ◽  
Sunney I. Chan
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Temperature Dependence ◽  
Cytochrome C Oxidase ◽  
Reduction Potential

scholarly journals Mitochondrial oxygenation of carbon monoxide

1986 ◽  
Vol 239 (1) ◽  
pp. 225-227 ◽  
Author(s):  
L J Young ◽  
W S Caughey
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
State University ◽  
Co Poisoning ◽  
Colorado State University

A variety of mitochondria have been observed to oxidize 13CO to 13CO2 in the presence of dioxygen, and on the basis of earlier studies [Young & Caughey (1986) Biochemistry 25, 152-161; Young (1981) Ph.D. Dissertation, Colorado State University] this activity is attributed to cytochrome c oxidase. Implications of these findings in respect of some aspects of the pathological biochemistry of CO poisoning are discussed.

Oxygenation of carbon monoxide by bovine heart cytochrome c oxidase

Biochemistry ◽  
1986 ◽  
Vol 25 (1) ◽  
pp. 152-161 ◽  
Author(s):  
Lawrence J. Young ◽  
Winslow S. Caughey
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Bovine Heart

scholarly journals Operando Infrared Spectroscopy for the Analysis of Gas-processing Metalloenzymes

2020 ◽  
Author(s):  
Sven Timo Stripp
Keyword(s):  
Infrared Spectroscopy ◽  
Cytochrome C ◽  
Ambient Temperature ◽  
Cytochrome C Oxidase ◽  
Structural Changes ◽  
Attenuated Total Reflection ◽  
Invasive Technique ◽  
Difference Spectra ◽  
Gas Processing ◽  
Temperature And Pressure

Earth-abundant transition metals like iron, nickel, copper, molybdenum, and vanadium have been identified as essential constituents of the cellular gas metabolism in all kingdoms of life. Associated with biological macromolecules, gas-processing metalloenzymes (GPMs) are formed that catalyse a variety of redox reactions. This includes the reduction of O2 to water by cytochrome c oxidase (‘complex IV’), the reduction of N2 to NH4 by nitrogenase, as well as the reduction of protons to H2 (and oxidation of the later) by hydrogenase. GPMs perform at ambient temperature and pressure, in the presence of water, and often extremely low educt concentrations, thus serving as natural examples for efficient catalysis. Facilitating the design of biomimetic catalysts, biophysicist thrive to understand the reaction principles of GPMs making use of various techniques. In this perspective, I will introduce Fourier-transform infrared spectroscopy in attenuated total reflection configuration (ATR FTIR) for the analysis of GPMs like cytochrome c oxidase, nitrogenase, and hydrogenase. Infrared spectroscopy provides information about the geometry and redox state of the catalytic cofactors, the protonation state of amino acid residues, the hydrogen-bonding network, and protein structural changes. I developed an approach to probe and trigger the reaction of GPMs by gas exchange experiments, exploring the reactivity of these enzymes with their natural reactants. This allows recording sensitive ATR FTIR difference spectra with seconds time resolution. Finally yet importantly, infrared spectroscopy is an electronically non-invasive technique that allows investigating protein samples under biologically relevant conditions, i.e., at ambient temperature and pressure, and in the presence of water.

Sign in / Sign up

Export Citation Format

Share Document