Research Topics
Genomes and Genes | Jonathan HoslerSummaryAffiliation: University of Mississippi Medical Center Country: USA Publications
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Publications
Energy transduction: proton transfer through the respiratory complexesJonathan P Hosler
Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, USA
Annu Rev Biochem 75:165-87. 2006..There is evidence for an important role of subunit III and proton backflow, but the number and nature of gating mechanisms remain elusive, as does the mechanism of physiological control of efficiency...
The influence of subunit III of cytochrome c oxidase on the D pathway, the proton exit pathway and mechanism-based inactivation in subunit IJonathan P Hosler
Department of Biochemistry, University of Mississippi Medical Center, 2500 N State Street, Jackson, MS 39216 4505, USA
Biochim Biophys Acta 1655:332-9. 2004..Analysis of proton pumping by subunit III-depleted oxidase forms leads to the proposal that the trapping of two protons in the D pathway, one on E286 and one on D132, is required for efficient proton pumping...
Altering conserved lipid binding sites in cytochrome c oxidase of Rhodobacter sphaeroides perturbs the interaction between subunits I and III and promotes suicide inactivation of the enzymeLakshman Varanasi
Department of Biochemistry, University of Mississippi Medical Center, 2500 North State Street, Jackson, Mississippi 39216, USA
Biochemistry 45:14896-907. 2006....
A role for subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidaseDenise A Mills
Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824, USA
Biochemistry 42:7410-7. 2003..Thus, subunit III appears to affect the transfer of protons from both the inner and outer surfaces of cytochrome oxidase, perhaps accounting for the long-observed lower efficiency of proton pumping by the subunit III-depleted oxidase...
Alternative initial proton acceptors for the D pathway of Rhodobacter sphaeroides cytochrome c oxidaseLakshman Varanasi
Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, United States
Biochemistry 50:2820-8. 2011..The results show how the environment of the initial proton acceptor for the D pathway in these CcO forms dictates the pH range of CcO activity, with implications for the function of Asp-132, the normal proton acceptor...
Disease-related mutations in cytochrome c oxidase studied in yeast and bacterial modelsMelyssa Bratton
Department of Biochemistry, University of Mississippi Medical Center, USA
Eur J Biochem 270:1222-30. 2003..The bacterial system allows detailed biochemical analysis of the effect of the mutations on the function and assembly of the catalytic core of the enzyme...
Assembly of cytochrome-c oxidase in the absence of assembly protein Surf1p leads to loss of the active site hemeDaniel Smith
Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216 4505, USA
J Biol Chem 280:17652-6. 2005..The results suggest that maturation of the heme a(3)-Cu(B) center is a step that limits the association of subunits I and II in the assembly of mitochondrial cytochrome oxidase...
Mutagenic analysis of Cox11 of Rhodobacter sphaeroides: insights into the assembly of Cu(B) of cytochrome c oxidaseAudie K Thompson
Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, USA
Biochemistry 49:5651-61. 2010..Rather, consideration of the properties of Lys-123 and the apparent specificity of Cox11 suggest that Lys-123 plays a role in the interaction of Cox11 with its target...
Evidence for a cytochrome bcc-aa3 interaction in the respiratory chain of Mycobacterium smegmatisJames A Megehee
Department of Microbiology, The University of Mississippi Medical Center, Jackson, 2500 North State Street, MS 39216-4505, USA
Microbiology 152:823-9. 2006..The results indicate that hydrophobic interactions are the primary forces maintaining the bcc-aa3 interaction, but ionic interactions may assist in aligning the two complexes for efficient electron transfer...
Detection of transient intermediates in the metal-dependent nonoxidative decarboxylation catalyzed by alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylaseTingfeng Li
Department of Biochemistry, The University of Mississippi Medical Center, Jackson, MS 39216, USA
J Am Chem Soc 129:9278-9. 2007
The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyaninJohn K Ma
Department of Biochemistry, University of Mississippi Medical Center, 2500 N State Street, Jackson, MS 39216 4505, United States
J Inorg Biochem 102:342-6. 2008..These results suggest that metal incorporation in vivo occurs during protein folding in the periplasm and not to a preformed type 1 site...
Slow proton transfer through the pathways for pumped protons in cytochrome c oxidase induces suicide inactivation of the enzymeDenise A Mills
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48109, USA
Biochemistry 44:4656-66. 2005..The experiments suggest that increased lifetimes of the heme a(3) oxoferryl intermediates as well as the anionic form of Glu286 of the D pathway cause suicide inactivation in the active site...
Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic propertiesChristopher J Carrell
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, Missouri 63110, USA
Biochemistry 46:1900-12. 2007....
Research Grants
- SUBUNIT III AND CYTOCHROME OXIDASE FUNCTIONJonathan Hosler; Fiscal Year: 2002....
- Role of Subunit III in Cytochrome Oxidase FunctionJonathan Hosler; Fiscal Year: 2007..The mechanism of this assembly process is likely to differ from the assembly of other copper centers in proteins since the active site of cytochrome oxidase is buried within subunit I and within the transmembrane region of the protein. ..
