Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo

Hosler, Jonathan P.; Ferguson‐Miller, Shelagh; Calhoun, Melissa W.; Thomas, Joyce; Hill, John J.; Lemieux, Laura J.; Ma, Jixiang; Georgiou, Christos D.; Fetter, John; Shapleigh, James P.; Tecklenburg, Mary M; Babcock, Gerald T.; Gennis, Robert B.

doi:10.1007/bf00762854

Cited by 264 publications

(250 citation statements)

References 73 publications

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“…Thus, it became apparent that there is a whole superfamily of related aerobic heme and Cu-containing oxidases [59], including now also quinol oxidases, which use a variety of heme components for the same purpose, i.e. oxygen reduction to H,O ; however, only the cytochrome c oxidases contained a Cu, site.…”

Section: Progress Through Advances In Related Fields Protein Chem-mentioning

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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Section: Progress Through Advances In Related Fields Protein Chem-mentioning

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 apparent variability in the q+/2e-yield of cytochrome cbb3 is not well understood at present. It has been observed, however, that certain regions in subunit I that are believed to be important for the coupling between oxygen reduction and proton pumping in cytochrome aa 3 and cytochrome bo3, e.g., the loop between helix II and III as well as helix VIII (Svensson et al, 1995;Hosler et al, 1992;Fetter et al, 1995;Thomas et al, 1994), are not very well conserved in cytochrome cbb3 .…”

Section: Efficiency Of Free-energy Transducingmentioning

confidence: 99%

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Spanning

Boer

Reijnders

et al. 1995

J Bioenerg Biomembr

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General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 12 May 2018Journal of Bioenergetics and Biomembranes, Vol. 27, No. 5, 1995 Received May 29, 1995 Paracoccus denitrificans is a facultative anaerobic bacterium that has the capacity to adjust its metabolic infrastructure, quantitatively and/or qualitatively, to the prevailing growth condition. In this bacterium the relative activity of distinct catabolic pathways is subject to a hierarchical control. In the presence of oxygen the aerobic respiration, the most efficient way of electron transfer-linked phosphorylation, has priority. At high oxygen tensions P. denitrificans synthesizes an oxidase with a relatively low affinity for oxygen, whereas under oxygen limitation a high-affinity oxidase appears specifically induced. During anaerobiosis, the pathways with lower free energy-transducing efficiency are induced. In the presence of nitrate, the expression of a number of dehydrogenases ensures the continuation of oxidative pbosphorylation via denitrification. After identification of the structural components that are involved in both the aerobic and the anaerobic respiratory networks of P. denitrificans, the intriguing next challenge is to get insight in its regulation. Two transcription regulators have recently been demonstrated to be involved in the expression of a number of aerobic and/or anaerobic respiratory complexes in P. denitrificans. Understanding of the regulation machinery is beginning to emerge and promises much excitement in discovery.KEY WORDS: Respiratory network; multiple oxidases; denitrification; gene regulation; FNR; Paracoccus denitrificans; Escherichia coli. ~TRODUCTIONThe ultimate goal of living organisms is to contribute to a continued existence of their species by means of survival and reproduction. In unicellular organisms, the ability to survive depends on the cell's potential to adapt its metabolism to the available carbon and free-energy sources in its natural habitat, ensuring maintenance and growth. The more such an environment is subject to fluctuations in the supply of these substrates, the higher the demands that are made upon the potential of the cell to adjust its metabolic properties. A profound example of this flexibility is the process of bacterial respiration...

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“…Six strictly conserved histidines (H) are involved in liganding the heme and copper cofactors (for reviews, see [3,10,11]). All of them are located at the periplasmic face of the membrane [8].…”

Section: Introductionmentioning

confidence: 99%

Histidine 131, not histidine 43, of the Bradyrhizobium japonicum FixN protein is exposed towards the periplasm and essential for the function of the cbb₃‐type cytochrome oxidase

1996

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In subunit I (FixN) of the Bradyrhizobiumjaponicum cbb3-type oxidase, only five instead of the normal six strictly conserved histidines (H) could be unambiguously assigned as the putative heme or copper ligands. The ambiguity concerned H43 or H131 as the presumptive N-terminal ligands of the low-spin heme B. We report here that a H43A replacement had a wildtype phenotype, whereas the H131A mutant was defective in oxidase function and suhunlt assembly or stability, suggesting that H131 serves as the N-terminal low-spin heine ligand. Topological studies revealed that H131 resides on the periplasmic side of helix 2, where one of the low-spin heme ligands is normally found in conventional heme-copper oxidases.

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Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo

Cited by 264 publications

References 73 publications

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

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

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Histidine 131, not histidine 43, of the Bradyrhizobium japonicum FixN protein is exposed towards the periplasm and essential for the function of the cbb₃‐type cytochrome oxidase

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Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo

Cited by 264 publications

References 73 publications

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

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

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Histidine 131, not histidine 43, of the Bradyrhizobium japonicum FixN protein is exposed towards the periplasm and essential for the function of the cbb3‐type cytochrome oxidase

Contact Info

Product

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Histidine 131, not histidine 43, of the Bradyrhizobium japonicum FixN protein is exposed towards the periplasm and essential for the function of the cbb₃‐type cytochrome oxidase