Analysis of Proton Transfer Reactions in the Cytochrome-C-Oxidase of Mitochondria

1982 ◽  
pp. 1201-1224
Author(s):  
S. Papa ◽  
F. Guerrieri ◽  
M. Lorusso ◽  
G. Izzo ◽  
F. Capuano ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Proton Transfer ◽  
Cytochrome C Oxidase ◽  
Transfer Reactions ◽  
Proton Transfer Reactions

Characteristics and nature of redox-linked proton transfer reactions in cytochrome c oxidase of mitochondria

1985 ◽  
Vol 23 (3-4) ◽  
pp. 317-325 ◽  
Author(s):  
Sergio Papa ◽  
Nazzareno Capitanio ◽  
Emanuele De Nitto ◽  
Gianfranco Izzo
Keyword(s):  
Cytochrome C ◽  
Proton Transfer ◽  
Cytochrome C Oxidase ◽  
Transfer Reactions ◽  
Proton Transfer Reactions

scholarly journals FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase

2004 ◽  
Vol 1655 ◽  
pp. 321-331 ◽  
Author(s):  
Benjamin H. McMahon ◽  
Marian Fabian ◽  
Farol Tomson ◽  
Timothy P. Causgrove ◽  
James A. Bailey ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Proton Transfer ◽  
Cytochrome C Oxidase ◽  
Transfer Reactions ◽  
Ftir Studies ◽  
Proton Transfer Reactions

scholarly journals Protonation Dynamics in the K-Channel of Cytochrome c Oxidase Estimated from Molecular Dynamics Simulations

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 265
Author(s):  
Vincent Stegmaier ◽  
Rene F. Gorriz ◽  
Petra Imhof
Keyword(s):  
Molecular Dynamics ◽  
Cytochrome C ◽  
Proton Transfer ◽  
Molecular Dynamics Simulations ◽  
Cytochrome C Oxidase ◽  
Proton Transport ◽  
K Channel ◽  
Proton Transfer Reactions ◽  
Dynamics Simulations ◽  
Hydrogen Bonded

Proton transfer reactions are one of the most fundamental processes in biochemistry. We present a simplistic approach for estimating proton transfer probabilities in a membrane protein, cytochrome c oxidase. We combine short molecular dynamics simulations at discrete protonation states with a Monte Carlo approach to exchange between those states. Requesting for a proton transfer the existence of a hydrogen-bonded connection between the two source and target residues of the exchange, restricts the acceptance of transfers to only those in which a proton-relay is possible. Together with an analysis of the hydrogen-bonded connectivity in one of the proton-conducting channels of cytochrome c oxidase, this approach gives insight into the protonation dynamics of the hydrogen-bonded networks. The connectivity and directionality of the networks are coupled to the conformation of an important protein residue in the channel, K362, rendering proton transfer in the entire channel feasible in only one of the two major conformations. Proton transport in the channel can thus be regulated by K362 not only through its possible role as a proton carrier itself, but also by allowing or preventing proton transport via water residues.

scholarly journals Effects of ion/ion proton transfer reactions on conformation of gas-phase cytochrome c ions

2010 ◽  
Vol 21 (7) ◽  
pp. 1208-1217 ◽  
Author(s):  
Qin Zhao ◽  
Gregg M. Schieffer ◽  
Matthew W. Soyk ◽  
Timothy J. Anderson ◽  
R. S. Houk ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Proton Transfer ◽  
Gas Phase ◽  
Transfer Reactions ◽  
Ion Proton ◽  
Proton Transfer Reactions
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