scholarly journals The redox-coupled proton-channel opening in cytochrome c oxidase

2020 ◽  
Vol 11 (15) ◽  
pp. 3804-3811
Author(s):  
Alexander Wolf ◽  
Jovan Dragelj ◽  
Juliane Wonneberg ◽  
Johannes Stellmacher ◽  
Jens Balke ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Long Range ◽  
Conformational Changes ◽  
Water Dynamics ◽  
Proton Channel ◽  
Channel Activation ◽  
Channel Opening ◽  
Bond Rearrangement

The interplay of cytochrome c oxidase's cofactor electrostatics, long-range conformational changes, H-bond rearrangement, and water dynamics enables transient proton-channel activation.

scholarly journals Interaction of Cytochrome C Oxidase with Steroid Hormones

Cells ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 2211
Author(s):  
Ilya P. Oleynikov ◽  
Natalia V. Azarkina ◽  
Tatiana V. Vygodina ◽  
Alexander A. Konstantinov
Keyword(s):  
Electron Transfer ◽  
Bile Acid ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Steroid Hormones ◽  
Peroxidase Activity ◽  
Spectral Shift ◽  
Proton Channel ◽  
Dodecyl Maltoside ◽  
Bile Acid Binding

Estradiol, testosterone and other steroid hormones inhibit cytochrome c oxidase (CcO) purified from bovine heart. The inhibition is strongly dependent on concentration of dodecyl-maltoside (DM) in the assay. The plots of Ki vs [DM] are linear for both estradiol and testosterone which may indicate an 1:1 stoichiometry competition between the hormones and the detergent. Binding of estradiol, but not of testosterone, brings about spectral shift of the oxidized CcO consistent with an effect on heme a33+. We presume that the hormones bind to CcO at the bile acid binding site described by Ferguson-Miller and collaborators. Estradiol is shown to inhibit intraprotein electron transfer between hemes a and a3. Notably, neither estradiol nor testosterone suppresses the peroxidase activity of CcO. Such a specific mode of action indicates that inhibition of CcO activity by the hormones is associated with impairing proton transfer via the K-proton channel.

scholarly journals Dewetting transitions coupled to K-channel activation in cytochrome c oxidase

2018 ◽  
Vol 9 (32) ◽  
pp. 6703-6710 ◽  
Author(s):  
Shreyas Supekar ◽  
Ville R. I. Kaila
Keyword(s):  
Free Energy ◽  
Cytochrome C ◽  
Oxygen Reduction ◽  
Cytochrome C Oxidase ◽  
Biological Membrane ◽  
Proton Gradient ◽  
K Channel ◽  
Channel Activation ◽  
Electrochemical Proton Gradient ◽  
Respiratory Chains

Cytochrome c oxidase (CcO) drives aerobic respiratory chains in all organisms by transducing the free energy from oxygen reduction into an electrochemical proton gradient across a biological membrane.

scholarly journals Suicide Inactivation in Rhodobacter Sphaeroides Cytochrome c Oxidase Lacking Subunit III Coincides with Release of CuB and Major Conformational Changes in Subunit I

2012 ◽  
Vol 102 (3) ◽  
pp. 574a
Author(s):  
Lawrence J. Prochaska ◽  
Robert R. Geyer ◽  
Jonathan P. Hosler ◽  
Audie Thompson ◽  
Lakshman Varanasi ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Conformational Changes ◽  
Rhodobacter Sphaeroides ◽  
Suicide Inactivation ◽  
Subunit Iii

scholarly journals 2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer

Metallomics ◽  
2011 ◽  
Vol 3 (6) ◽  
pp. 619 ◽  
Author(s):  
Christoph Nowak ◽  
Thamara Laredo ◽  
Jens Gebert ◽  
Jacek Lipkowski ◽  
Robert B. Gennis ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Conformational Changes ◽  
Direct Electron Transfer

Hydrogen-Bonded Network and Water Dynamics in the D-channel of Cytochrome c Oxidase

2018 ◽  
Vol 251 (3) ◽  
pp. 299-314 ◽  
Author(s):  
Tahereh Ghane ◽  
Rene F. Gorriz ◽  
Sandro Wrzalek ◽  
Senta Volkenandt ◽  
Ferand Dalatieh ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Water Dynamics ◽  
Hydrogen Bonded
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