Biological Oxidations

Massey, Vincent; Veeger, C.

doi:10.1146/annurev.bi.32.070163.003051

Cited by 38 publications

(12 citation statements)

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“…Well-known flavin photomodifications, first reported a half century ago, include the photolysis of the ribityl chain of flavin mononucleotide (FMN) to produce the N10 dealkylated species, lumichrome 117,118 , or the N10 methylated species lumiflavin 119 . In both cases, ribityl photolysis is catalyzed by a highly-oxidizing triplet intermediate on the flavin isoalloxazine moiety formed via intersystem crossing from a singlet excited state.…”

Section: Figurementioning

confidence: 99%

Function, structure and mechanism of bacterial photosensory LOV proteins

2011

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LOV domains are protein photosensors conserved in bacteria, archaea, plants and fungi that detect blue light via a flavin cofactor. In the bacterial kingdom, LOV domains are present in both chemotrophic and phototrophic species, where they are found N-terminally of signaling and regulatory domains such as sensor histidine kinases, diguanylate cyclases/phosphodiesterases, DNA-binding domains, and σ factor regulators. In this review, we describe the current state of knowledge on the function of bacterial LOV proteins, the structural basis of LOV domain-mediated signal transduction, and the use of LOV domains as genetically-encoded photoswitches in synthetic biology.

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Section: Figurementioning

confidence: 99%

Function, structure and mechanism of bacterial photosensory LOV proteins

2011

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“…There was a distinct progression of attitudes toward the problem. While Massey and Veeger concluded in their 1963 Annual Reviews article [25] that 'The question of the role of Cu in COX remains extremely controversial...', Malmstrom and Neilands, in their 1964 review article [16] stated that '...the involvement of Cuz+ in the catalytic reaction is by no means excluded, but instead seems rather likely, as the redox processes are very rapid with natural substrates,' so that even those opposed to the Biochem. 245) idea that there were e-carriers in the respiratory chain in addition to those then identified, considered the problem at least worth further study by that time [26].…”

Section: Copper In Cox and Its Historymentioning

confidence: 99%

Copper A of Cytochrome c Oxidase, A Novel, Long‐Embattled, Biological Electron‐Transfer Site

Beinert

1997

European Journal of Biochemistry

124

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This review traces the history of understanding of the CU, site in cytochrome c oxidase (COX) from the beginnings, when few believed that there was any significant Cu in COX, to the verification of three atoms Cu/monomer and to the final identification of the site as a dinuclear, Cys-bridged average valence ... Cu' 5+ structure through spectroscopy, recombinant DNA techniques, and crystallography. The CUM+ critical steps forward in understanding the nature of the Cu, site are recounted and the present state (as of the end of 1996) of our knowledge of the molecular and electronic structure is discussed in some detail. The contributions made through the years by the development of methodology and concepts for solving the enigma of Cu, are emphasized and impediments, often rooted in contemporary preconceptions and attitudes rather than solid data, are mentioned, which discouraged the exploitation of early valuable clues. Finally, analogies in construction principles of polynuclear Cu-S and Fe-S proteins are pointed out.

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“…The hydroxyl radical is produced directly both in the xanthine oxidase reaction [17] and also by stimulated PMNLs [18]. Another possibility is that the nonenzymatic action of iron in lysosomes with hydrogen peroxide, which is also produced both in the xanthine oxidase reaction [19] and by stimulated PMNLs [20,21], to form hydroxyl radicals may have contributed to lysosomal damage. Polyamines which show a scavenging action were found to give some protection against the lytic action of oxygen products on lysosomes.…”

Section: Discussionmentioning

confidence: 99%