Zobrazeno 1 - 8
of 8
pro vyhledávání: '"J A Garcia-Horsman"'
Publikováno v:
Biochemistry. 34:4428-4433
The ubiquinol oxidase, cytochrome bo3, of Escherichia coli is a member of the respiratory heme-copper oxidase family and conserves energy from the reduction of dioxygen to water by translocation of protons across the bacterial membrane. Mutation of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::452722ae2b3ac3f0cb55db4ebfb4da4b
https://doi.org/10.1021/bi00013a035
https://doi.org/10.1021/bi00013a035
Publikováno v:
Europe PubMed Central
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b53c25826814ff3c5a2d3f32c7c833d
https://doi.org/10.1128/jb.176.18.5587-5600.1994
https://doi.org/10.1128/jb.176.18.5587-5600.1994
Autor:
Laura Lemieux, John Walter Hill, Goswitz Vc, Melissa W. Calhoun, Gennis Rb, James O. Alben, J A Garcia-Horsman
Publikováno v:
Biochemistry. 31:11435-11440
Amino acid sequence data have revealed that the bo-type ubiquinol oxidase from Escherichia coli is closely related to the eukaryotic aa3-type cytochrome c oxidases. In the cytochrome c oxidases, the reduction of oxygen to water occurs at a binuclear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::276d273f40d155aa1b04505dd49dda77
https://doi.org/10.1021/bi00161a023
https://doi.org/10.1021/bi00161a023
Autor:
M, Käenmäki, A, Tammimäki, J A, Garcia-Horsman, T, Myöhänen, N, Schendzielorz, M, Karayiorgou, J A, Gogos, P T, Männistö
Publikováno v:
British journal of pharmacology. 158(8)
Catechol-O-methyltransferase (COMT) metabolizes compounds containing catechol structures and has two forms: soluble (S-COMT) and membrane-bound (MB-COMT). Here we report the generation of a mouse line that expresses MB-COMT but not S-COMT. We compare
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ccb72273ec93faa6b5b0e6ce8ca16b2e
https://pubmed.ncbi.nlm.nih.gov/19930170
https://pubmed.ncbi.nlm.nih.gov/19930170
Autor:
Robert B. Gennis, J. Arturo Garcia-Horsman, Laura Lemieux, James O. Alben, Melissa W. Calhoun, Jeffrey W. Thomas
Publikováno v:
FEBS letters. 368(3)
A common feature within the heme-copper oxidase superfamily is the dinuclear heme-copper center. Analysis via extended X-ray absorption fine structure (EXAFS) has led to the proposal that sulfur may be bound to CU B , a component of the dinuclear cen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::639389e46665a74d3842b1757fb46619
https://pubmed.ncbi.nlm.nih.gov/7635213
https://pubmed.ncbi.nlm.nih.gov/7635213
Resonance Raman spectra are reported on ferric, ferrous, and cyanide-bound cytochrome cbb3 oxidase, and compared with other heme b and heme c containing enzymes. These spectra are used to assess the spin and ligation states of the hemes via the porph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8189ca4ae7a178963e38564eec4291e
https://hdl.handle.net/20.500.14279/2218
https://hdl.handle.net/20.500.14279/2218
Publikováno v:
Biochemistry. 33(10)
Rhodobacter sphaeroides contains at least two different cytochrome c oxidases. When these bacteria are grown with high aeration, the traditional aa3-type cytochrome c oxidase is present at relatively high levels. However, under microaerophilic growth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e3cd7bd28df6f4bb76cb093d3db53bf
https://pubmed.ncbi.nlm.nih.gov/8130226
https://pubmed.ncbi.nlm.nih.gov/8130226
Publikováno v:
European journal of biochemistry. 199(3)
Two aa3-type cytochromes were purified from membranes of sporulating Bacillus cereus. One of them, an aa3 complex, was found to be composed of two subunits (51 and 31 kDa), two a hemes and three copper atoms, thus being similar to the cytochrome aa3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be67314282d99b03feffc574a0f04499
https://pubmed.ncbi.nlm.nih.gov/1651246
https://pubmed.ncbi.nlm.nih.gov/1651246