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  1. Article ; Online: Time-Resolved Electrometric Study of the F→O Transition in Cytochrome c Oxidase. The Effect of Zn

    Siletsky, Sergey A / Gennis, Robert B

    Biochemistry. Biokhimiia

    2021  Volume 86, Issue 1, Page(s) 105–122

    Abstract: The effect of Zn2+ on the P-side of proteoliposomes containing membrane-incorporated Rhodobacter sphaeroides cytochrome c oxidase was investigated by the time-resolved electrometrics following a single electron injection into the enzyme prepared in the F ...

    Abstract The effect of Zn2+ on the P-side of proteoliposomes containing membrane-incorporated Rhodobacter sphaeroides cytochrome c oxidase was investigated by the time-resolved electrometrics following a single electron injection into the enzyme prepared in the F state. The wild-type enzyme was examined along with the two mutants, N139D and D132N. All obtained data indicate that the primary effect of Zn2+ added from the P-side of the membrane is slowing of the pumped proton release from the proton loading site (PLS) to the bulk aqueous phase on the P-side of the membrane. The results strongly suggest the presence of two pathways by which the pumped proton can exit the protein from the PLS and of two separate binding sites for Zn2+. A model is presented to explain the influence of Zn2+ on the kinetics of membrane-potential generation by the wild-type COX, as well as by the N139D and D132N mutants.
    MeSH term(s) Cations, Divalent ; Electron Transport Complex IV/metabolism ; Kinetics ; Proton Pumps ; Rhodobacter sphaeroides/enzymology ; Rhodobacter sphaeroides/metabolism ; Zinc/chemistry ; Zinc/metabolism
    Chemical Substances Cations, Divalent ; Proton Pumps ; Electron Transport Complex IV (EC 1.9.3.1) ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2021-03-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1109-5
    ISSN 1608-3040 ; 0006-2979 ; 0320-9717
    ISSN (online) 1608-3040
    ISSN 0006-2979 ; 0320-9717
    DOI 10.1134/S0006297921010107
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  2. Article ; Online: Structures of the intermediates in the catalytic cycle of mitochondrial cytochrome c oxidase.

    Wikström, Mårten / Gennis, Robert B / Rich, Peter R

    Biochimica et biophysica acta. Bioenergetics

    2022  Volume 1864, Issue 2, Page(s) 148933

    MeSH term(s) Electron Transport Complex IV/metabolism ; Mitochondria/metabolism ; Catalysis
    Chemical Substances Electron Transport Complex IV (EC 1.9.3.1)
    Language English
    Publishing date 2022-11-17
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbabio.2022.148933
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  3. Article ; Online: Evolution of quinol oxidation within the heme‑copper oxidoreductase superfamily.

    Murali, Ranjani / Hemp, James / Gennis, Robert B

    Biochimica et biophysica acta. Bioenergetics

    2022  Volume 1863, Issue 8, Page(s) 148907

    Abstract: The heme‑copper oxidoreductase (HCO) superfamily is a large superfamily of terminal respiratory enzymes that are widely distributed across the three domains of life. The superfamily includes biochemically diverse oxygen reductases and nitric oxide ... ...

    Abstract The heme‑copper oxidoreductase (HCO) superfamily is a large superfamily of terminal respiratory enzymes that are widely distributed across the three domains of life. The superfamily includes biochemically diverse oxygen reductases and nitric oxide reductases that are pivotal in the pathways of aerobic respiration and denitrification. The adaptation of HCOs to use quinol as the electron donor instead of cytochrome c has significant implication for the respiratory flexibility and energetic efficiency of the respiratory chains that include them. In this work, we explore the adaptation of this scaffold to two different electron donors, cytochromes c and quinols, with extensive sequence analysis of these enzymes from publicly available datasets. Our work shows that quinol oxidation evolved independently within the HCO superfamily at least seven times. Enzymes from only two of these independently evolved clades have been biochemically well-characterized. Combining structural modeling with sequence analysis, we identify putative quinol binding sites in each of the novel quinol oxidases. Our analysis of experimental and modeling data suggests that the quinol binding site appears to have evolved at the same structural position within the scaffold more than once.
    MeSH term(s) Copper ; Cytochromes c ; Heme/metabolism ; Hydroquinones/chemistry ; Nitric Oxide/metabolism ; Oxidoreductases/metabolism ; Oxygen/metabolism
    Chemical Substances Hydroquinones ; Nitric Oxide (31C4KY9ESH) ; Heme (42VZT0U6YR) ; Copper (789U1901C5) ; Cytochromes c (9007-43-6) ; Oxidoreductases (EC 1.-) ; Oxygen (S88TT14065) ; hydroquinone (XV74C1N1AE)
    Language English
    Publishing date 2022-08-06
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbabio.2022.148907
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  4. Article ; Online: Proton Dynamics at the Membrane Surface.

    Gennis, Robert B

    Biophysical journal

    2016  Volume 110, Issue 9, Page(s) 1909–1911

    Language English
    Publishing date 2016--10
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2016.04.001
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  5. Article ; Online: Evolution of the cytochrome bd oxygen reductase superfamily and the function of CydAA' in Archaea.

    Murali, Ranjani / Gennis, Robert B / Hemp, James

    The ISME journal

    2021  Volume 15, Issue 12, Page(s) 3534–3548

    Abstract: ... CydAA' is the first isoform of cytbd containing only b-type hemes shown to be active when isolated ...

    Abstract Cytochrome bd-type oxygen reductases (cytbd) belong to one of three enzyme superfamilies that catalyze oxygen reduction to water. They are widely distributed in Bacteria and Archaea, but the full extent of their biochemical diversity is unknown. Here we used phylogenomics to identify three families and several subfamilies within the cytbd superfamily. The core architecture shared by all members of the superfamily consists of four transmembrane helices that bind two active site hemes, which are responsible for oxygen reduction. While previously characterized cytochrome bd-type oxygen reductases use quinol as an electron donor to reduce oxygen, sequence analysis shows that only one of the identified families has a conserved quinol binding site. The other families are missing this feature, suggesting that they use an alternative electron donor. Multiple gene duplication events were identified within the superfamily, resulting in significant evolutionary and structural diversity. The CydAA' cytbd, found exclusively in Archaea, is formed by the co-association of two superfamily paralogs. We heterologously expressed CydAA' from Caldivirga maquilingensis and demonstrated that it performs oxygen reduction with quinol as an electron donor. Strikingly, CydAA' is the first isoform of cytbd containing only b-type hemes shown to be active when isolated from membranes, demonstrating that oxygen reductase activity in this superfamily is not dependent on heme d.
    MeSH term(s) Archaea/enzymology ; Archaea/genetics ; Archaeal Proteins/genetics ; Cytochrome b Group/genetics ; Electron Transport Chain Complex Proteins/genetics ; Evolution, Molecular ; Oxidation-Reduction ; Oxidoreductases/genetics ; Oxygen
    Chemical Substances Archaeal Proteins ; Cytochrome b Group ; Electron Transport Chain Complex Proteins ; Oxidoreductases (EC 1.-) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2021-06-18
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2406536-5
    ISSN 1751-7370 ; 1751-7362
    ISSN (online) 1751-7370
    ISSN 1751-7362
    DOI 10.1038/s41396-021-01019-4
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    Z 7773: Show issues

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  6. Article ; Online: Single-particle cryo-EM studies of transmembrane proteins in SMA copolymer nanodiscs.

    Sun, Chang / Gennis, Robert B

    Chemistry and physics of lipids

    2019  Volume 221, Page(s) 114–119

    Abstract: Styrene-maleic acid (SMA) copolymers can extract membrane proteins from native membranes along with lipids as nanodiscs. Preparation with SMA is fast, cost-effective, and captures the native protein-lipid interactions. On the other hand, cryo-EM has ... ...

    Abstract Styrene-maleic acid (SMA) copolymers can extract membrane proteins from native membranes along with lipids as nanodiscs. Preparation with SMA is fast, cost-effective, and captures the native protein-lipid interactions. On the other hand, cryo-EM has become increasingly successful and efficient for structural determinations of membrane proteins, with biochemical sample preparation often the bottleneck. Three recent cryo-EM studies on the efflux transporter AcrB and the alternative complex III: cyt c oxidase supercomplex have demonstrated the potential of SMA nanodisc samples to yield high-resolution structure information of membrane proteins.
    MeSH term(s) Cryoelectron Microscopy ; Maleates/chemistry ; Models, Molecular ; Nanoparticles/chemistry ; Particle Size ; Polymers/chemistry ; Styrene/chemistry ; Surface Properties
    Chemical Substances Maleates ; Polymers ; Styrene (44LJ2U959V) ; maleic acid (91XW058U2C)
    Language English
    Publishing date 2019-03-30
    Publishing country Ireland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 213869-4
    ISSN 1873-2941 ; 0009-3084
    ISSN (online) 1873-2941
    ISSN 0009-3084
    DOI 10.1016/j.chemphyslip.2019.03.007
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  7. Article: Functional importance of Glutamate-445 and Glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli.

    Murali, Ranjani / Gennis, Robert B

    Biochimica et biophysica acta. Bioenergetics

    2018  Volume 1859, Issue 8, Page(s) 577–590

    Abstract: ... of the three heme components, heme d and heme b ...

    Abstract The recent X-ray structure of the cytochrome bd respiratory oxygen reductase showed that two of the three heme components, heme d and heme b
    MeSH term(s) Cell Respiration ; Cytochromes/chemistry ; Cytochromes/genetics ; Cytochromes/metabolism ; Electron Transport ; Electron Transport Chain Complex Proteins/chemistry ; Electron Transport Chain Complex Proteins/genetics ; Electron Transport Chain Complex Proteins/metabolism ; Electrons ; Escherichia coli/growth & development ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Glutamic Acid/chemistry ; Glutamic Acid/genetics ; Glutamic Acid/metabolism ; Heme/chemistry ; Heme/metabolism ; Mutagenesis, Site-Directed ; Mutation ; Oxidation-Reduction ; Oxidoreductases/chemistry ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Oxygen/chemistry ; Protons
    Chemical Substances Cytochromes ; Electron Transport Chain Complex Proteins ; Escherichia coli Proteins ; Protons ; Glutamic Acid (3KX376GY7L) ; Heme (42VZT0U6YR) ; Oxidoreductases (EC 1.-) ; cytochrome bd terminal oxidase complex, E coli (EC 1.9.3.-) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2018-04-30
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0005-2728 ; 0006-3002 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0005-2728 ; 0006-3002 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbabio.2018.04.012
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  8. Article: Evolution of quinol oxidation within the heme‑copper oxidoreductase superfamily

    Murali, Ranjani / Hemp, James / Gennis, Robert B.

    Biochimica et biophysica acta. 2022 Aug. 02,

    2022  

    Abstract: The heme‑copper oxidoreductase (HCO) superfamily is a large superfamily of terminal respiratory enzymes that are widely distributed across the three domains of life. The superfamily includes biochemically diverse oxygen reductases and nitric oxide ... ...

    Abstract The heme‑copper oxidoreductase (HCO) superfamily is a large superfamily of terminal respiratory enzymes that are widely distributed across the three domains of life. The superfamily includes biochemically diverse oxygen reductases and nitric oxide reductases that are pivotal in the pathways of aerobic respiration and denitrification. The adaptation of HCOs to use quinol as the electron donor instead of cytochrome c has significant implication for the respiratory flexibility and energetic efficiency of the respiratory chains that include them. In this work, we explore the adaptation of this scaffold to two different electron donors, cytochromes c and quinols, with extensive sequence analysis of these enzymes from publicly available datasets. Our work shows that quinol oxidation evolved independently within the HCO superfamily at least seven times. Enzymes from only two of these independently evolved clades have been biochemically well-characterized. Combining structural modeling with sequence analysis, we identify putative quinol binding sites in each of the novel quinol oxidases. Our analysis of experimental and modeling data suggests that the quinol binding site appears to have evolved at the same structural position within the scaffold more than once.
    Keywords aerobiosis ; cytochrome c ; data collection ; denitrification ; energy efficiency ; evolution ; nitric oxide ; oxidation ; oxidoreductases ; oxygen ; sequence analysis
    Language English
    Dates of publication 2022-0802
    Publishing place Elsevier B.V.
    Document type Article
    Note Pre-press version
    ZDB-ID 282711-6
    ISSN 0005-2728 ; 0304-4173
    ISSN 0005-2728 ; 0304-4173
    DOI 10.1016/j.bbabio.2022.148907
    Database NAL-Catalogue (AGRICOLA)

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  9. Book: Biomembranes

    Gennis, Robert B.

    molecular structure and function

    (Springer advanced texts in chemistry)

    1989  

    Series title Springer advanced texts in chemistry
    Keywords Cell Membrane ; Biomembran ; Struktur
    Subject Biologische Membran ; Einheitsmembran ; Zelle ; Zellmembran
    Language English
    Size XVII, 533 S. : Ill., zahlr. graph. Darst.
    Publisher Springer
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT003282768
    ISBN 3-540-96760-5 ; 0-387-96760-5 ; 978-3-540-96760-6 ; 978-0-387-96760-8
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    1989 A 5998 order for loan Magazin

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  10. Article ; Online: Specific inhibition of proton pumping by the T315V mutation in the K channel of cytochrome ba

    Siletsky, Sergey A / Soulimane, Tewfik / Belevich, Ilya / Gennis, Robert B / Wikström, Mårten

    Biochimica et biophysica acta. Bioenergetics

    2021  Volume 1862, Issue 9, Page(s) 148450

    Abstract: Cytochrome ... ...

    Abstract Cytochrome ba
    MeSH term(s) Cytochrome b Group/metabolism ; Electron Transport Complex IV/metabolism ; Heme/metabolism ; Models, Molecular ; Mutant Proteins/metabolism ; Mutation ; Oxidation-Reduction ; Oxidoreductases/metabolism ; Oxygen/metabolism ; Potassium Channels/metabolism ; Protein Binding ; Protein Conformation ; Proton Pumps/metabolism ; Thermus thermophilus/metabolism
    Chemical Substances Cytochrome b Group ; Mutant Proteins ; Potassium Channels ; Proton Pumps ; Heme (42VZT0U6YR) ; Oxidoreductases (EC 1.-) ; cytochrome ba3 (EC 1.-) ; copper oxidase (EC 1.16.-) ; Electron Transport Complex IV (EC 1.9.3.1) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2021-05-20
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbabio.2021.148450
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