Zobrazeno 1 - 10
of 96
pro vyhledávání: '"Masakazu Hirasawa"'
Autor:
Roger Bryan Sutton, David B. Knaff, Nanditha Vaidyanathan, Masakazu Hirasawa, Anurag P. Srivastava, Jacaranda Solis, R. Max Wynn
Based on in silico docking methods, five amino acids in glutamate synthase (Gln-467, His-1144, Asn-1147, Arg-1162, and Trp-676) likely constitute key binding residues in the interface of a glutamate synthase:ferredoxin complex. Although all interfaci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81e323055786297825d9552e9b3adb98
https://europepmc.org/articles/PMC5995153/
https://europepmc.org/articles/PMC5995153/
Autor:
Patrick J. Farmer, Shane Tappa, Shu-Fen Lu, Mirko Zaffagnini, Jatindra N. Tripathy, Sabeeha S. Merchant, Masakazu Hirasawa, Aimee M. Terauchi, Stéphane D. Lemaire, David B. Knaff, Toshiharu Hase
Publikováno v:
Journal of Biological Chemistry. 284:25867-25878
Ferredoxin (Fd) is the major iron-containing protein in photosynthetic organisms and is central to reductive metabolism in the chloroplast. The Chlamydomonas reinhardtii genome encodes six plant type [Fe2S2] ferredoxins, products of PETF, FDX2-FDX6.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41605a40373e878539c3504c3d1b4b31
https://doi.org/10.1074/jbc.m109.023622
https://doi.org/10.1074/jbc.m109.023622
Autor:
Michael K. Johnson, Masakazu Hirasawa, Megha Bhalla, David B. Knaff, Ramasamy Somasundaram, Jatindra N. Tripathy, James P. Allen
Publikováno v:
Molecular Plant. 2(3):407-415
A series of site-directed mutants of the ferredoxin-dependent spinach nitrite reductase has been characterized and several amino acids have been identified that appear to be involved in the interaction of the enzyme with ferredoxin. In a complementar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d12523d54eb1692a7184b0449389d9c
Autor:
Bernard Lagoutte, Nicolas Cassan, Masakazu Hirasawa, Pierre Sétif, David B. Knaff, Jatindra N. Tripathy
Publikováno v:
Biochemistry. 48:2828-2838
Nitrite reductase, which reduces nitrite to ammonium in a six-electron reaction, was characterized through kinetic analysis of an electron transfer cascade involving photoexcited Photosystem I and ferredoxin. This cascade was studied at physiological
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7002f4a24b624005559f3cf0a8b19608
https://doi.org/10.1021/bi802096f
https://doi.org/10.1021/bi802096f
Autor:
Sung Kun Kim, David B. Knaff, James P. Allen, Masakazu Hirasawa, Aaron T. Setterdahl, Jatindra N. Tripathy
Publikováno v:
Photosynthesis Research. 94:1-12
A system has been developed for expressing a His-tagged form of the ferredoxin-dependent nitrite reductase of spinach in Escherichia coli. The catalytic and spectral properties of the His-tagged, recombinant enzyme are similar, but not identical, to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cffccbb4130ee20993da42d129767c3f
https://doi.org/10.1007/s11120-007-9198-5
https://doi.org/10.1007/s11120-007-9198-5
Autor:
Sung Kun Kim, Masami Kusunoki, Masakazu Hirasawa, Toshiharu Hase, Hideaki Unno, José M. Gualberto, Lluis Masip, Michael K. Johnson, Sibali Bandyopadhyay, George Georgiou, Nicolas Rouhier, Virginie Lattard, David B. Knaff, Jean-Pierre Jacquot
Publikováno v:
Proceedings of the National Academy of Sciences. 104:7379-7384
When expressed in Escherichia coli , cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron–sulfur-containing holoprotein or as a monomeric apoprotein in solution. Analytical and spectroscopic studies of wild-type protein and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbca1620778c41d1dbc5c92347eac327
https://doi.org/10.1073/pnas.0702268104
https://doi.org/10.1073/pnas.0702268104
Autor:
Michael K. Johnson, Masakazu Hirasawa, Anurag P. Srivastava, Brian J. Vaccaro, David B. Knaff, James P. Allen, Suzanne Alkul
An in silico model of the ferredoxin-dependent nitrate reductase from the cyanobacterium Synechococcus sp. PCC 7942, and information about active sites in related enzymes, had identified Cys148, Met149, Met306, Asp163, and Arg351 as amino acids likel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ec32b8d6c90cabd388231d286ac6299
https://europepmc.org/articles/PMC4638386/
https://europepmc.org/articles/PMC4638386/
Autor:
Afia Dasgupta, Francisco J. Florencio, Masoud Zabet-Moghaddam, David B. Knaff, Jatindra N. Tripathy, R. Bryan Sutton, Masakazu Hirasawa, Nanditha Vaidyanathan, Anurag P. Srivastava
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
idUS. Depósito de Investigación de la Universidad de Sevilla
instname
idUS. Depósito de Investigación de la Universidad de Sevilla
It had been proposed that a loop, typically containing 26 or 27 amino acids, which is only present in monomeric, ferredoxin-dependent, “plant-type” glutamate synthases and is absent from the catalytic α-subunits of both NADPH-dependent, heterodi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b889bda4ca6492444660b979ad142289
http://hdl.handle.net/10261/110753
http://hdl.handle.net/10261/110753
Autor:
David B. Knaff, Sung Kun Kim, Michael K. Johnson, Varinnia Gomes, Thomas Leustek, Jeremy T. Mason, Masakazu Hirasawa, Richard C. Conover, Mace L. Moore, Afroza Rahman
Publikováno v:
Biochemistry. 45:5010-5018
The 5'-adenylyl sulfate (APS) reductase from the marine macrophytic green alga Enteromorpha intestinalis uses reduced glutathione as the electron donor for the reduction of APS to 5'-AMP and sulfite. The E. intestinalis enzyme (EiAPR) is composed of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de821cb4ebbe7aabeb04617aba870688
https://doi.org/10.1021/bi0519250
https://doi.org/10.1021/bi0519250
Autor:
Masakazu Hirasawa, Uma Swamy, Sung Kun Kim, Jatinda N. Tripathy, Meitian Wang, James P. Allen, David B. Knaff
Publikováno v:
Biochemistry. 44:16054-16063
The structure of nitrite reductase, a key enzyme in the process of nitrogen assimilation, has been determined using X-ray diffraction to a resolution limit of 2.8 A. The protein has a globular fold consisting of 3 alpha/beta domains with the siroheme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e6953598dd27995888ab625832c9027
https://doi.org/10.1021/bi050981y
https://doi.org/10.1021/bi050981y