Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Sandip K. Badyal"'
Autor:
Andrea, Gumiero, Andrea, Guimero, Sandip K, Badyal, Tina, Leeks, Peter C E, Moody, Emma Lloyd, Raven
Publikováno v:
Dalton Trans.. 42:3170-3175
We have previously demonstrated (Badyal et al., J. Biol. Chem., 2006, 281, 24512) that removal of the active site tryptophan (Trp41) in ascorbate peroxidase increases the conformational mobility of the distal histidine residue (His42) and that His42
Autor:
Isabel K. Macdonald, Clive Metcalfe, Sandip K. Badyal, Igor Efimov, Peter C. E. Moody, Emma Lloyd Raven, Andrea Gumiero
We test the hypothesized pathway by which protons are passed from the substrate, ascorbate, to the ferryl oxygen in the heme enzyme ascorbate peroxidase (APX). The role of amino acid side chains and bound solvent is demonstrated. We investigated solv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2badd05122d763b9d2cd39518ab3eb55
https://ora.ox.ac.uk/objects/uuid:66723f50-9e3c-4f1b-b866-dcd3347aaf63
https://ora.ox.ac.uk/objects/uuid:66723f50-9e3c-4f1b-b866-dcd3347aaf63
Autor:
Zoi Pipirou, Clive M. Metcalfe, Emma Lloyd Raven, Andrew R. Bottrill, Sandip K. Badyal, Sharad Mistry, Bernard J. Rawlings
Electronic spectroscopy, HPLC analyses, and mass spectrometry (MALDI-TOF and MS/MS) have been used to show that a covalent link from the heme to the distal Trp41 can occur on exposure of ascorbate peroxidase (APX) to H2O2 under noncatalytic condition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f7a3e1f62ae1486ff0ff8267f8e107a
https://doi.org/10.1021/bi062274q
https://doi.org/10.1021/bi062274q
Autor:
Clive R. Bagshaw, Igor L. Barsukov, Jaswir Basran, Remigio Picone, Andrew F. Irvine, Hyun Suk Jung, Kaeko Tozawa, Lu-Yun Lian, Sandip K. Badyal, Martyna W. Pastok, Paul R. Elliott, Philip S. Rudland, Marina Kriajevska, Roger Barraclough
Publikováno v:
Structure(London, England:1993)
Summary Filament assembly of nonmuscle myosin IIA (NMIIA) is selectively regulated by the small Ca2+-binding protein, S100A4, which causes enhanced cell migration and metastasis in certain cancers. Our NMR structure shows that an S100A4 dimer binds t
Autor:
Sandip K. Badyal, Nina Bhanji, Hyun Suk Jung, Igor L. Barsukov, Ju Hwan Kim, Jaswir Basran, Andrew F. Irvine, Roger Craig, Alap P. Chavda, Paul R. Elliott, Clive R. Bagshaw, Marina Kriajevska
Publikováno v:
Journal of Molecular Biology. 405:1004-1026
The interaction between the calcium-binding protein S100A4 and the C-terminal fragments of nonmuscle myosin heavy chain IIA has been studied by equilibrium and kinetic methods. Using site-directed mutants, we conclude that Ca2+ binds to the EF2 domai
Autor:
M. Gordon Joyce, Isabel K. Macdonald, Harriet E. Seward, Katherine H. Sharp, Peter C. E. Moody, Sandip K. Badyal, Martin Mewies, Emma Lloyd Raven, Jaswir Basran
Publikováno v:
Journal of Biological Chemistry. 281:24512-24520
Conformational mobility of the distal histidine residue has been implicated for several different heme peroxidase enzymes, but unambiguous structural evidence is not available. In this work, we present mechanistic, spectroscopic, and structural evide
Autor:
Sandip K, Badyal, Jaswir, Basran, Nina, Bhanji, Ju Hwan, Kim, Alap P, Chavda, Hyun Suk, Jung, Roger, Craig, Paul R, Elliott, Andrew F, Irvine, Igor L, Barsukov, Marina, Kriajevska, Clive R, Bagshaw
Publikováno v:
Journal of Molecular Biology
The interaction between the calcium-binding protein S100A4 and the C-terminal fragments of nonmuscle myosin heavy chain IIA has been studied by equilibrium and kinetic methods. Using site-directed mutants, we conclude that Ca2+ binds to the EF2 domai
Autor:
Sandip K. Badyal, Clive Metcalfe, Jaswir Basran, Zoi Pipirou, Emma Lloyd Raven, Peter C. E. Moody, Andrea Gumiero, Sandeep Handa, Graham Eaton, Sharad Mistry
Publikováno v:
Biochemistry. 48(22)
The heme peroxidase and heme oxygenase enzymes share a common heme prosthetic group but catalyze fundamentally different reactions, the first being H(2)O(2)-dependent oxidation of substrate using an oxidized Compound I intermediate, and the second O(
Autor:
Sandip K. Badyal, Emma Lloyd Raven, Jaswir Basran, Igor Efimov, Peter C. E. Moody, Clive Metcalfe
Publikováno v:
Biochemistry. 47(15)
We have previously shown [Badyal, S. K., et al. (2006) J. Biol. Chem. 281, 24512-24520] that the distal histidine (His42) in the W41A variant of ascorbate peroxidase binds to the heme iron in the ferric form of the protein but that binding of the sub
Autor:
Kirsty J. McLean, Emma Lloyd Raven, Nektaria D. Papadopoulou, Andrew W. Munro, Igor Efimov, Isabel K. Macdonald, Peter C. E. Moody, Sandip K. Badyal
Publikováno v:
Biochemistry. 46(27)
Reduction potentials for the catalytic compound I/compound II and compound II/Fe3+ redox couples, and for the two-electron compound I/Fe3+ redox couple, have been determined for ascorbate peroxidase (APX) and for a number of site-directed variants. F