B. Hill

发表

Aryl radical involvement in amiodarone-induced pulmonary toxicity: investigation of protection by spin-trapping nitrones.

Takashi Takahashi, T. Massey, L. Bedard, 2007, Toxicology and applied pharmacology.

Electron transfer kinetics during the reduction and turnover of the cytochrome caa3 complex from Bacillus subtilis.

B. Hill, M. Assempour, D. Lim, 1998, Biochemistry.

Interactions of sulphide and other ligands with cytochrome c oxidase. An electron-paramagnetic-resonance study.

P. Nicholls, A. Thomson, B. Hill, 1984, The Biochemical journal.

The nature of haem a3 in the oxidized state of cytochrome c oxidase. Evidence from low-temperature magnetic-circular-dichroism spectroscopy in the near infrared region.

A. Thomson, B. Hill, C. Greenwood, 1982, The Biochemical journal.

Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase with oxygen.

B. Hill, 1994, The Journal of biological chemistry.

The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen.

B. Hill, 1991, The Journal of biological chemistry.

Quenching of intrinsic fluorescence of yeast cytochrome c peroxidase by covalently- and noncovalently-bound quenchers.

T. Fox, A. English, B. Hill, 1993, Biochemistry.

Cyanide binding to different redox states of the cytochrome caa3 complex from Bacillus subtilis; a member of the cytochrome oxidase super-family of enzymes

B. Hill, M. Assempour, 1997 .

Exposure of Bacillus subtilis to silver inhibits activity of cytochrome c oxidase in vivo via interaction with SCO, the CuA assembly protein.

B. Hill, S. Hussain, D. Andrews, 2018, Metallomics : integrated biometal science.

Stability of oxidized, reduced and copper bound forms of Bacillus subtilis Sco.

B. Hill, David E Davidson, 2009, Biochimica et biophysica acta.

The optical properties of CuA in bovine cytochrome c oxidase determined by low-temperature magnetic-circular-dichroism spectroscopy.

A. Thomson, D. Barber, B. Hill, 1983, The Biochemical journal.

Low temperature magnetic circular dichroism spectra and magnetization properties of extracted heme a3+ bis-imidazole. A model of cytochrome a in bovine cytochrome c oxidase.

A. Thomson, B. Hill, C. Greenwood, 1984, Journal of inorganic biochemistry.

Pathways of cytochrome c oxidation by soluble and membrane-bound cytochrome aa3.

P. Nicholls, J. Wrigglesworth, B. Hill, 1980, Canadian journal of biochemistry.

The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature. Evidence for new pathways of electron transfer.

B. Hill, C. Greenwood, 1984, The Biochemical journal.

Spectroscopic evidence for the participation of compound A (Fea32+-O2) in the reaction of mixed-valence cytochrome c oxidase with oxygen at room temperature.

B. Hill, C. Greenwood, 1983, The Biochemical journal.

Detection, characterization, and quenching of the intrinsic fluorescence of bovine heart cytochrome c oxidase.

P. Horowitz, N. C. Robinson, B. Hill, 1986, Biochemistry.

The structure of the cytochrome a3-CuB site of mammalian cytochrome c oxidase as probed by MCD and EPR spectroscopy.

P. Nicholls, A. Thomson, B. Hill, 1985, Journal of inorganic biochemistry.

The sequence of electron carriers in the reaction of cytochromec oxidase with oxygen

B. Hill, 1993, Journal of bioenergetics and biomembranes.

Spectral and cyanide binding properties of the cytochrome aa3 (600 nm) complex from Bacillus subtilis.

B. Hill, J. Peterson, 1998, Archives of biochemistry and biophysics.

Reversal of Cyanide Inhibition of Cytochrome c Oxidase by the Auxiliary Substrate Nitric Oxide

Jim Peterson, Bruce C Hill, Linda L Pearce, 2003, Journal of Biological Chemistry.

Effect of diethyl pyrocarbonate modification on spectral and steady-state kinetic properties of bovine heart cytochrome oxidase.

J. Doran, B. Hill, 1992, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Intermediate steps in the reaction of cytochrome oxidase with molecular oxygen.

P. Nicholls, B. Hill, C. Greenwood, 1986, Biochimica et biophysica acta.

The influence of temperature and osmolyte on the catalytic cycle of cytochrome c oxidase.

M. Marden, B. Hill, J. Kornblatt, 2003, European journal of biochemistry.

Characterization of a structural model of membrane bound cytochrome c-550 from Bacillus subtilis.

P. David, B. Wathen, B. Hill, 2000, Archives of biochemistry and biophysics.

Avoiding premature oxidation during the binding of Cu(II) to a dithiolate site in BsSCO. A rapid freeze‐quench EPR study

B. Bennett, B. Hill, 2011, FEBS letters.

Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase.

B. Yachnin, B. Hill, Katherine C. Yam, 2005, Biochemistry.

Identification of a disulfide switch in BsSco, a member of the Sco family of cytochrome c oxidase assembly proteins.

Z. Jia, Q. Ye, B. Hill, 2005, Biochemistry.

Characterization of YpmQ, an Accessory Protein Required for the Expression of Cytochrome c Oxidase in Bacillus subtilis *

B. Hill, N. R. Mattatall, Joanna Jazairi, 2000, The Journal of Biological Chemistry.

Using Tryptophan Mutants To Probe the Structural and Functional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis.

B. Hill, S. Hussain, D. Andrews, 2017, Biochemistry.

Chronic Treatment with Azide in Situ Leads to an Irreversible Loss of Cytochrome c Oxidase Activity via Holoenzyme Dissociation*

D. Glerum, Scot C Leary, Bruce C Hill, 2002, The Journal of Biological Chemistry.

Direct mitochondrial dysfunction precedes reactive oxygen species production in amiodarone-induced toxicity in human peripheral lung epithelial HPL1A cells.

Takashi Takahashi, T. Massey, J. Brien, 2008, Toxicology and applied pharmacology.

The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli.

R. Gennis, B. Hill, J. Hill, 1994, Biochemistry.

Electron Transfer from Cytochrome c to O2 a

B. Hill, 1988, Annals of the New York Academy of Sciences.

Reduction and activity of cytochrome c in the cytochrome c-cytochrome aa3 complex.

P. Nicholls, B. Hill, 1980, The Biochemical journal.

Expression, Purification, and Characterization of Recombinant Forms of Membrane-Bound Cytochromec-550nm fromBacillus subtilis

P. David, B. Hill, M. Morrison, 1999 .

Purification, crystallization and preliminary X-ray analysis of a Sco1-like protein from Bacillus subtilis, a copper-binding protein involved in the assembly of cytochrome c oxidase.

Z. Jia, Q. Ye, B. Hill, 2003, Acta crystallographica. Section D, Biological crystallography.

Formamide probes a role for water in the catalytic cycle of cytochrome c oxidase.

B. Hill, Yu Liu, 2007, Biochimica et biophysica acta.

The pathway of CO binding to cytochrome c oxidase Can the gateway be closed?

B. Hill, 1994, FEBS letters.

Copper binding traps the folded state of the SCO protein from Bacillus subtilis.

B. Hill, Katherine C. Yam, D. Andrews, 2012, Biochimica et biophysica acta.

Expression, purification, and characterization of the CuA-cytochrome c domain from subunit II of the Bacillus subtilis cytochrome caa3 complex in Escherichia coli.

B. Hill, D. Andrews, N. R. Mattatall, 2005, Protein expression and purification.

Cyanide binding to bovine heart cytochrome c oxidase depleted of subunit III by treatment with lauryl maltoside.

N. C. Robinson, B. Hill, N. Robinson, 1986, The Journal of biological chemistry.

Detergent modulation of electron and proton transfer reactions in bovine cytochrome c oxidase.

M. Tarasev, B. Hill, 2002, Archives of biochemistry and biophysics.

Intermediate forms of cytochrome oxidase observed in transient kinetic experiments and those visited in the catalytic cycle.

B. Hill, 2004, Biochimica et biophysica acta.

Differential affinity of BsSCO for Cu(II) and Cu(I) suggests a redox role in copper transfer to the Cu(A) center of cytochrome c oxidase.

B. Hill, D. Andrews, 2012, Biochimica et biophysica acta.

The affinity of yeast and bacterial SCO proteins for CU(I) and CU(II). A capture and release strategy for copper transfer

Shuai Xu, B. Hill, D. Andrews, 2015, Biochemistry and biophysics reports.

Reactivity of ligand-swapped mutants of the SCO protein from Bacillus subtilis. Isomers of the CCH metal binding motif.

X. Yao, B. Hill, D. Andrews, 2014, Biochimica et biophysica acta.

High-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes.

J. Albanese, B. Hill, W. Henning, 1995, The Biochemical journal.

Characterization of reductant-induced, tryptophan fluorescence changes in cytochrome oxidase.

B. Hill, L. Ferreira-Rajabi, 1989, Biochemistry.

Stopped-flow, laser-flash photolysis studies on the reactions of CO and O2 with the cytochrome caa3 complex from Bacillus subtilis: conservation of electron transfer pathways from cytochrome c to O2.

B. Hill, 1996, Biochemistry.

Differential affinity of BsSCO for Cu(II) and Cu(I) suggests a redox role in copper transfer to the Cu(A) center of cytochrome c oxidase.

B. Hill, D. Andrews, 2012, Biochimica et biophysica acta.

Photochemical and ligand-exchange properties of the cyanide complex of fully reduced cytochrome c oxidase.

S. Marmor, B. Hill, 1991, The Biochemical journal.