Snapshot of an oxygen intermediate in the catalytic reaction of cytochrome<i>c</i>oxidase

Ishigami, Izumi; Lewis-Ballester, Ariel; Echelmeier, Austin; Brehm, Gerrit; Zatsepin, Nadia A.; Grant, Thomas D.; Coe, Jesse; Lisova, Stella; Nelson, Garrett; Zhang, Shangji; Dobson, Zachary; Boutet, Sébastien; Sierra, Raymond G.; Batyuk, A.; Fromme, Petra; Fromme, Raimund; Spence, John C. H.; Ros, Alexandra; Yeh, Syun Ru; Rousseau, Denis L.

doi:10.1073/pnas.1814526116

Cited by 80 publications

(83 citation statements)

References 42 publications

(56 reference statements)

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“…While NORs use exclusively heme b and bind iron (Fe B ) in their nonheme center with a conserved 3His-1Glu first coordination sphere, HCOs may host different types of hemes (e.g., heme o, a, and b) and bind copper (Cu B ) with a tripodal 3His coordination sphere, depending on the organism [73]. Thorough mechanistic studies have been performed for these two homologous classes of proteins [74][75][76][77][78][79] and few details are still under debate [80][81][82]. Nonetheless, in both cases protein matrix is able to promote selectivity of one metal over the other and to drive the correct inter-metal distance along the various oxidation states of the metal and reaction intermediates [83].…”

Section: Figmentioning

confidence: 99%

Mimochrome, a metalloporphyrin‐based catalytic Swiss knife†

Leone

Chino

Nastri

et al. 2020

Biotech and App Biochem

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Over the years, mimochromes, a class of miniaturized porphyrin‐based metalloproteins, have proven to be reliable but still versatile scaffolds. After two decades from their birth, we retrospectively review our work in mimochrome design and engineering, which allowed us developing functional models. They act as electron‐transfer miniproteins or more elaborate artificial metalloenzymes, endowed with peroxidase, peroxygenase, and hydrogenase activities. Mimochromes represent simple yet functional synthetic models that respond to metal ion replacement and noncovalent modulation of the environment, similarly to natural heme‐proteins. More recently, we have demonstrated that the most active analogue retains its functionality when immobilized on nanomaterials and surfaces, thus affording bioconjugates, useful in sensing and catalysis. This review also briefly summarizes the most important contributions to heme‐protein design from leading groups in the field.

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Section: Figmentioning

confidence: 99%

Mimochrome, a metalloporphyrin‐based catalytic Swiss knife†

Leone

Chino

Nastri

et al. 2020

Biotech and App Biochem

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“…The catalytic cycle of O 2 reduction to water molecules (H 2 O) is shown from R to E H state. This cyclic model is proposed by Ishigami et al (23). We obtained the kind permission of the corresponding author to use part of their figure initially in their study.…”

Section: Resultsmentioning

confidence: 99%

Targeting Mitochondrial Singlet Oxygen Dynamics Offers New Perspectives for Effective Metabolic Therapies of Cancer

2020

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The occurrence of mitochondrial respiration has allowed evolution toward more complex and advanced life forms. However, its dysfunction is now also seen as the most probable cause of one of the biggest scourges in human health, cancer. Conventional cancer treatments such as chemotherapy, which mainly focus on disrupting the cell division process, have shown being effective in the attenuation of various cancers but also showing significant limits as well as serious sides effects. Indeed, the idea that cancer is a metabolic disease with mitochondria as the central site of the pathology is now emerging, and we provide here a review supporting this "novel" hypothesis re-actualizing past century Otto Warburg's thoughts. Our conclusion, while integrating literature, is that mitochondrial activity and, in particular, the activity of cytochrome c oxidase, complex IV of the ETC, plays a fundamental role in the effectiveness or non-effectiveness of chemotherapy, immunotherapy and probably radiotherapy treatments. We therefore propose that cancer cells mitochondrial singlet oxygen (1 O 2) dynamics may be an efficient target for metabolic therapy development.

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“…Normal electron transfer rates have been reported for all three variants, as would be expected for ideally uncoupled oxidases. These data, together with redox-and ligand-induced structural changes in two domains of the H-channel (56)(57)(58)(59), have led to the proposal that it is the H-channel that provides the route for pumped protons both into and out of the proton trap. However, mutagenesis of H-channel residues of bacterial HCOs failed to support any crucial H-channel function.…”

Section: Discussionmentioning

confidence: 99%

A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria

Maréchal

Genko

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

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Mitochondria metabolize almost all the oxygen that we consume, reducing it to water by cytochrome c oxidase (CcO). CcO maximizes energy capture into the protonmotive force by pumping protons across the mitochondrial inner membrane. Forty years after the H+/e− stoichiometry was established, a consensus has yet to be reached on the route taken by pumped protons to traverse CcO’s hydrophobic core and on whether bacterial and mitochondrial CcOs operate via the same coupling mechanism. To resolve this, we exploited the unique amenability to mitochondrial DNA mutagenesis of the yeast Saccharomyces cerevisiae to introduce single point mutations in the hydrophilic pathways of CcO to test function. From adenosine diphosphate to oxygen ratio measurements on preparations of intact mitochondria, we definitely established that the D-channel, and not the H-channel, is the proton pump of the yeast mitochondrial enzyme, supporting an identical coupling mechanism in all forms of the enzyme.

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Snapshot of an oxygen intermediate in the catalytic reaction of cytochromecoxidase

Cited by 80 publications

References 42 publications

Mimochrome, a metalloporphyrin‐based catalytic Swiss knife†

Mimochrome, a metalloporphyrin‐based catalytic Swiss knife†

Targeting Mitochondrial Singlet Oxygen Dynamics Offers New Perspectives for Effective Metabolic Therapies of Cancer

A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria

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