Next Article in Journal
Synthesis, Crystal Structure, Electrochemistry and Electro-Catalytic Properties of the Manganese-Containing Polyoxotungstate, [(Mn(H2O)3)2(H2W12O42)]6−
Next Article in Special Issue
Modelling the (Essential) Role of Proton Transport by Electrolyte Bases for Electrochemical Water Oxidation at Near-Neutral pH
Previous Article in Journal
Cytotoxic Gold(I) Complexes with Amidophosphine Ligands Containing Thiophene Moieties
Previous Article in Special Issue
Design of Molecular Water Oxidation Catalysts Stabilized by Ultrathin Inorganic Overlayers—Is Active Site Protection Necessary?
Open AccessReview

Tracing the Pathways of Waters and Protons in Photosystem II and Cytochrome c Oxidase

1
Department of Physics, City College of New York, New York, NY 10031, USA
2
Ph.D. Program in Chemistry, The Graduate Center of the City University of New York, New York, NY 10016, USA
3
Ph.D. Program in Physics, The Graduate Center of the City University of New York, New York, NY 10016, USA
*
Author to whom correspondence should be addressed.
The first two authors contributed equally to this paper.
Inorganics 2019, 7(2), 14; https://doi.org/10.3390/inorganics7020014
Received: 1 January 2019 / Revised: 25 January 2019 / Accepted: 28 January 2019 / Published: 31 January 2019
(This article belongs to the Special Issue Recent Advances in Water Oxidation Catalysis)
Photosystem II (PSII) uses water as the terminal electron donor, producing oxygen in the Mn4CaO5 oxygen evolving complex (OEC), while cytochrome c oxidase (CcO) reduces O2 to water in its heme–Cu binuclear center (BNC). Each protein is oriented in the membrane to add to the proton gradient. The OEC, which releases protons, is located near the P-side (positive, at low-pH) of the membrane. In contrast, the BNC is in the middle of CcO, so the protons needed for O2 reduction must be transferred from the N-side (negative, at high pH). In addition, CcO pumps protons from N- to P-side, coupled to the O2 reduction chemistry, to store additional energy. Thus, proton transfers are directly coupled to the OEC and BNC redox chemistry, as well as needed for CcO proton pumping. The simulations that study the changes in proton affinity of the redox active sites and the surrounding protein at different states of the reaction cycle, as well as the changes in hydration that modulate proton transfer paths, are described. View Full-Text
Keywords: proton pumping; network analysis; proton affinity; proton coupled electron transfer proton pumping; network analysis; proton affinity; proton coupled electron transfer
Show Figures

Figure 1

MDPI and ACS Style

Kaur, D.; Cai, X.; Khaniya, U.; Zhang, Y.; Mao, J.; Mandal, M.; Gunner, M.R. Tracing the Pathways of Waters and Protons in Photosystem II and Cytochrome c Oxidase. Inorganics 2019, 7, 14.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop