A Functional Model of Cytochrome c Oxidase: Thermodynamic Implications

Collman, James P.; Fu, Lei; Herrmann, Paul C.; Wang, Zhong; Rapta, Miroslav; Bröring, Martin; Schwenninger, Reinhold; Boitrel, Bernard

doi:10.1002/(sici)1521-3773(19981231)37:24<3397::aid-anie3397>3.0.co;2-n

Cited by 62 publications

(7 citation statements)

References 11 publications

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“…With the use of binuclear Fe II -Cu I complexes 9 and 10 (Figure ), Collman and co-workers demonstrated that the state of the bound peroxo was very sensitive to the nature of the Cu I -coordinating site. Complex 9 predominately catalyzes the two-electron reduction of O 2 to H 2 O 2 , whereas 10 catalyzes the four-electron reduction of O 2 to H 2 O under physiological conditions . The 4e – ORR with catalysts on the graphite disk electrode can be written as eqs –. …”

Section: Oxygen Reduction Reactionmentioning

confidence: 99%

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Energy-Related Small Molecule Activation Reactions: Oxygen Reduction and Hydrogen and Oxygen Evolution Reactions Catalyzed by Porphyrin- and Corrole-Based Systems

2016

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Globally increasing energy demands and environmental concerns related to the use of fossil fuels have stimulated extensive research to identify new energy systems and economies that are sustainable, clean, low cost, and environmentally benign. Hydrogen generation from solar-driven water splitting is a promising strategy to store solar energy in chemical bonds. The subsequent combustion of hydrogen in fuel cells produces electric energy, and the only exhaust is water. These two reactions compose an ideal process to provide clean and sustainable energy. In such a process, a hydrogen evolution reaction (HER), an oxygen evolution reaction (OER) during water splitting, and an oxygen reduction reaction (ORR) as a fuel cell cathodic reaction are key steps that affect the efficiency of the overall energy conversion. Catalysts play key roles in this process by improving the kinetics of these reactions. Porphyrin-based and corrole-based systems are versatile and can efficiently catalyze the ORR, OER, and HER. Because of the significance of energy-related small molecule activation, this review covers recent progress in hydrogen evolution, oxygen evolution, and oxygen reduction reactions catalyzed by porphyrins and corroles.

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Section: Oxygen Reduction Reactionmentioning

confidence: 99%

Section: Oxygen Reduction Reactionmentioning

confidence: 99%

Energy-Related Small Molecule Activation Reactions: Oxygen Reduction and Hydrogen and Oxygen Evolution Reactions Catalyzed by Porphyrin- and Corrole-Based Systems

2016

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“…Several synthetic model complexes have been developed to mimic the c NOR active site. Some of the first mimics for c NORs were model complexes that were originally designed for heme-copper oxidases, and the Cu was subsequently replaced by a non-heme Fe center. ,,− The first heme/non-heme diiron dinitrosyl complex was synthesized by Karlin and coworkers, using a TPP 2– derivative for the heme, with a covalently-linked TMPA (tris(methylpyridyl)amine) ligand to mimic the Fe B site (see Figure , left) . While this complex was able to generate a diferrous dinitrosyl complex, it was not able to catalyze the reduction of NO to N 2 O .…”

Section: The Nitrogen Cyclementioning

confidence: 99%

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

et al. 2021

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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 with iron, is at the heart of many biological transformations involving NO. A series of heme proteins, nitric oxide synthases (NOS), soluble guanylate cyclase (sGC), and nitrophorins, are responsible for the biosynthesis, sensing, and transport of NO. Alternatively, NO can be generated from nitrite by heme- and copper-containing nitrite reductases (NIRs). The NO-bearing small molecules such as nitrosothiols and dinitrosyl iron complexes (DNICs) can serve as an alternative vehicle for NO storage and transport. Once NO is formed, the rich reaction chemistry of NO leads to a wide variety of biological activities including reduction of NO by heme or non-heme iron-containing NO reductases and protein post-translational modifications by DNICs. Much of our understanding of the reactivity of metal sites in biology with NO and the mechanisms of these transformations has come from the elucidation of the geometric and electronic structures and chemical reactivity of synthetic model systems, in synergy with biochemical and biophysical studies on the relevant proteins themselves. This review focuses on recent advancements from studies on proteins and model complexes that not only have improved our understanding of the biological roles of NO but also have provided foundations for biomedical research and for bio-inspired catalyst design in energy science.

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“…In addition to spectroscopic studies, the stoichiometric reactivity of these species toward exogenous reductants, acid sources, and hydrogen atom donors (H + + e – ) has been evaluated to gauge their reactivity properties. The electrocatalytic O 2 -reduction with heme–Cu catalysts in fact has proven to be very successful, especially from the systematic studies carried out by Collman and co-workers. ,,,, Insights can and have probed aspects such as the role of the Cu ion, pH effects, solvent polarity influences, and how rates of electron flux (from an electrode) govern O 2 -reduction efficiency.…”

Section: Small Molecule Synthetic Models Of Heme-copper Oxidasesmentioning

confidence: 99%

Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function

et al. 2018

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Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial respiratory electron transport chain, which utilize a unique heterobinuclear active site to catalyze the 4H+/4e− reduction of dioxygen to water. This process involves a proton-coupled electron transfer (PCET) from a tyrosine (phenolic) residue and additional redox events coupled to transmembrane proton pumping and ATP synthesis. Given that HCOs are large, complex, membrane-bound enzymes, bioinspired synthetic model chemistry is a promising approach to better understand heme-Cu-mediated dioxygen reduction, including the details of proton and electron movements. This review encompasses important aspects of heme-O2 and copper–O2 (bio)chemistries as they relate to the design and interpretation of small molecule model systems and provides perspectives from fundamental coordination chemistry, which can be applied to the understanding of HCO activity. We focus on recent advancements from studies of heme–Cu models, evaluating experimental and computational results, which highlight important fundamental structure–function relationships. Finally, we provide an outlook for future potential contributions from synthetic inorganic chemistry and discuss their implications with relevance to biological O2-reduction.

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A Functional Model of Cytochrome c Oxidase: Thermodynamic Implications

Cited by 62 publications

References 11 publications

Energy-Related Small Molecule Activation Reactions: Oxygen Reduction and Hydrogen and Oxygen Evolution Reactions Catalyzed by Porphyrin- and Corrole-Based Systems

Energy-Related Small Molecule Activation Reactions: Oxygen Reduction and Hydrogen and Oxygen Evolution Reactions Catalyzed by Porphyrin- and Corrole-Based Systems

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function

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