Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kuppala V. Narasimhulu"'
Autor:
Dmitriy Lukoyanov, Zhi Yong Yang, Brian M. Hoffman, Kuppala V. Narasimhulu, Sergei A. Dikanov, Dennis R. Dean, Brett M. Barney, Rimma I. Samoilova, Lance C. Seefeldt
Publikováno v:
Journal of the American Chemical Society. 133:11655-11664
Enzymatic N(2) reduction proceeds along a reaction pathway composed of a sequence of intermediate states generated as a dinitrogen bound to the active-site iron-molybdenum cofactor (FeMo-co) of the nitrogenase MoFe protein undergoes six steps of hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b34247fc4ffcc47a11fdec002216df3
https://doi.org/10.1021/ja2036018
https://doi.org/10.1021/ja2036018
Autor:
Sergei A. Dikanov, Robert B. Gennis, Sophia M. Yi, Kuppala V. Narasimhulu, Rimma I. Samoilova
Publikováno v:
Journal of Biological Chemistry. 285:18241-18251
Cytochrome aa(3)-600 is one of the principle respiratory oxidases from Bacillus subtilis and is a member of the heme-copper superfamily of oxygen reductases. This enzyme catalyzes the two-electron oxidation of menaquinol and the four-electron reducti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95857a0ccbee82eed0aedc0398923b0d
https://doi.org/10.1074/jbc.m110.116186
https://doi.org/10.1074/jbc.m110.116186
Publikováno v:
Photosynthesis Research. 96:51-60
We have developed a rapid method for isolation of the Photosystem I (PS1) complex from Chlamydomonas reinhardtii using epitope tagging. Six histidine residues were genetically added to the N-terminus of the PsaA core subunit of PS1. The His(6)-tagged
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efcf887bf27053b887d4158087383ec7
https://doi.org/10.1007/s11120-007-9283-9
https://doi.org/10.1007/s11120-007-9283-9
Publikováno v:
Journal of the American Chemical Society. 129:5391-5402
Concanavalin A is a member of the plant hemeagglutinin (or plant lectin) family that contains two metal binding sites; one, called S1, is occupied by Mn2+ and the other, S2, by Ca2+. 55Mn electron-nuclear double resonance (ENDOR) measurements were pe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::231fc4a1045d80636996eb6a2d49bb71
https://doi.org/10.1021/ja0662826
https://doi.org/10.1021/ja0662826
Publikováno v:
Magnetic Resonance in Chemistry. 43:S40-S50
The properties of the Mn2+ site in the protein concanavalin A were investigated by single crystal W-band EPR/ENDOR (electron-nuclear double resonance) measurements. Initially, room temperature EPR measurements were carried out, one type of Mn2+ was i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a09d0aa675d4c6c50aad60f810e860be
https://doi.org/10.1002/mrc.1668
https://doi.org/10.1002/mrc.1668
Autor:
Jian-Ying Miao, Kuppala V Narasimhulu, Ping-I Lin, Lian-Pin Hwang, Sheng Hsien Lin, Dennis W. Hwang, Yit-Tsong Chen
Publikováno v:
Carbon. 42:813-822
Carbon spheres with diameters between 400 and 2000 nm were synthesized in large quantities by catalytic chemical vapor deposition (CCVD) method using Kaolin supported transition metal salts (M=Fe, Co, Ni, etc.) as catalysts. The reaction conditions f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b48da696aada0c26621402dcda46fe9
https://doi.org/10.1016/j.carbon.2004.01.053
https://doi.org/10.1016/j.carbon.2004.01.053
Autor:
Kuppala V. Narasimhulu, Amgalanbaatar Baldansuren, Lai Lai Yap, Sergei A. Dikanov, Robert B. Gennis, Sylvia K. Choi, Myat T. Lin, Patrick J. O'Malley, Rimma I. Samoilova, Richard Hart
Publikováno v:
Biochemistry. 51(18)
Selective (15)N isotope labeling of the cytochrome bo(3) ubiquinol oxidase from Escherichia coli with auxotrophs was used to characterize the hyperfine couplings with the side-chain nitrogens from residues R71, H98, and Q101 and peptide nitrogens fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ffe1946d57bb9cfe5a6539f303cd2aa
https://pubmed.ncbi.nlm.nih.gov/22497216
https://pubmed.ncbi.nlm.nih.gov/22497216
Autor:
Robert B. Gennis, Alexander A. Shubin, Sergei A. Dikanov, Amgalanbaatar Baldansuren, Kuppala V. Narasimhulu, Rimma I. Samoilova, Myat T. Lin
The cytochrome bo(3) ubiquinol oxidase from Escherichia coli resides in the bacterial cytoplasmic membrane and catalyzes the two-electron oxidation of ubiquinol-8 and four-electron reduction of O(2) to water. The one-electron reduced semiquinone form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81041f070505f9dbb669510db9a02b17
https://europepmc.org/articles/PMC3060462/
https://europepmc.org/articles/PMC3060462/
