The biologically relevant coordination chemistry of iron and nitric oxide: electronic structure and reactivity

N Lehnert, E Kim, HT Dong, JB Harland… - Chemical …, 2021 - ACS Publications
Nitric oxide (NO) is an important signaling molecule that is involved in a wide range of
physiological and pathological events in biology. Metal coordination chemistry, especially …

Synthetic Fe/Cu complexes: toward understanding heme-copper oxidase structure and function

SM Adam, GB Wijeratne, PJ Rogler, DE Diaz… - Chemical …, 2018 - ACS Publications
Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochrome c oxidase

C Safari, S Ghosh, R Andersson, J Johannesson… - Science …, 2023 - science.org
Cytochrome c oxidase (C c O) is part of the respiratory chain and contributes to the
electrochemical membrane gradient in mitochondria as well as in many bacteria, as it uses …

High-resolution XFEL structure of the soluble methane monooxygenase hydroxylase complex with its regulatory component at ambient temperature in two oxidation …

V Srinivas, R Banerjee, H Lebrette… - Journal of the …, 2020 - ACS Publications
Soluble methane monooxygenase (sMMO) is a multicomponent metalloenzyme that
catalyzes the conversion of methane to methanol at ambient temperature using a nonheme …

High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Environment

T Tiefenbrunn, W Liu, Y Chen, V Katritch, CD Stout… - PloS one, 2011 - journals.plos.org
The fundamental chemistry underpinning aerobic life on Earth involves reduction of
dioxygen to water with concomitant proton translocation. This process is catalyzed by …

Redox-Dependent Conformational Changes in Cytochrome c Oxidase Suggest a Gating Mechanism for Proton Uptake

L Qin, J Liu, DA Mills, DA Proshlyakov, C Hiser… - Biochemistry, 2009 - ACS Publications
A role for conformational change in the coupling mechanism of cytochrome c oxidase is the
subject of controversy. Relatively small conformational changes have been reported in …

Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature

I Ishigami, NA Zatsepin, M Hikita… - Proceedings of the …, 2017 - National Acad Sciences
Cytochrome c oxidase (C c O), the terminal enzyme in the electron transfer chain,
translocates protons across the inner mitochondrial membrane by harnessing the free …

The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states

C Coelho, PJ González, JJG Moura, I Moura… - Journal of molecular …, 2011 - Elsevier
The periplasmic nitrate reductase (NapAB) from Cupriavidus necator is a heterodimeric
protein that belongs to the dimethyl sulfoxide reductase family of mononuclear Mo …

Carbon Monoxide Dehydrogenase Reaction Mechanism: A Likely Case of Abnormal CO2 Insertion to a Ni−H Bond

P Amara, JM Mouesca, A Volbeda… - Inorganic …, 2011 - ACS Publications
Ni-containing carbon monoxide dehydrogenases (CODH), present in many anaerobic
microorganisms, catalyze the reversible oxidation of CO to CO2 at the so-called C-cluster …

[HTML][HTML] Gating and regulation of the cytochrome c oxidase proton pump

S Ferguson-Miller, C Hiser, J Liu - Biochimica et Biophysica Acta (BBA) …, 2012 - Elsevier
As a consumer of 95% of the oxygen we breathe, cytochrome c oxidase plays a major role in
the energy balance of the cell. Regulation of its oxygen reduction and proton pumping …