Zobrazeno 1 - 10
of 1 207
pro vyhledávání: '"Mauk Ag"'
Publikováno v:
Biochemistry. 41:11495-11503
Myoglobin (Mb) catalyzes a range of oxidation reactions in the presence of hydrogen peroxide (H(2)O(2)) through a peroxidase-like cycle. C110A and Y103F variants of human Mb have been constructed to assess the effects of removing electron-rich oxidiz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f49a524cbdbe9557e1f9d196bb3f54a2
https://doi.org/10.1021/bi025835w
https://doi.org/10.1021/bi025835w
Publikováno v:
Inorganic Chemistry. 40:5017-5023
Both electron paramagnetic resonance (EPR) and electronic absorption spectroscopy have been employed to investigate the reaction of a guanine-rich DNA nucleotide-hemin complex (PS2.M-hemin complex) and organic peroxide (t-Bu-OOH). Incubation of the P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1fa965178ea5f89dfb82517db1d460c
https://doi.org/10.1021/ic010025e
https://doi.org/10.1021/ic010025e
Publikováno v:
Journal of the American Chemical Society. 123:1337-1348
A specific DNA oligonucleotide--hemin complex (PS2.M--hemin complex) that exhibits DNA-enhanced peroxidative activity was studied by EPR and UV--visible spectroscopy and by chemical probing analysis. EPR data obtained from low-temperature experiments
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90530920cff68f6fe95ca2627b8a39c1
https://doi.org/10.1021/ja0023534
https://doi.org/10.1021/ja0023534
Autor:
Ryan Pauls, Alex Hillar, Brian Peters, Haoming Zhang, Peter C. Loewen, Mauk Ag, Alexander Loboda
Publikováno v:
Biochemistry. 39:5868-5875
Catalase-peroxidases have a predominant catalatic activity but differ from monofunctional catalases in exhibiting a substantial peroxidatic reaction which has been implicated in the activation of the antitubercular drug isoniazid in Mycobacterium tub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a4f4ed4c84bba44f08d63f362bfa4e9
https://doi.org/10.1021/bi0000059
https://doi.org/10.1021/bi0000059
Autor:
Mauk Ag
Publikováno v:
Essays in Biochemistry. 34:101-124
A wide range of biological processes makes extensive use of electron-transfer reactions. Rigorous characterization of a biological electron-transfer reaction requires a combination of kinetic, thermodynamic, structural and theoretical methods. The ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3328be5b80c3f886cf3481e352f9fdbc
https://doi.org/10.1042/bse0340101
https://doi.org/10.1042/bse0340101
Publikováno v:
Proceedings of the National Academy of Sciences. 95:12825-12831
Random mutagenesis and screening for enzymatic activity has been used to engineer horse heart myoglobin to enhance its intrinsic peroxidase activity. A chemically synthesized gene encoding horse heart myoglobin was subjected to successive cycles of P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::284c2c615baedfb09d6416156d58c73e
https://doi.org/10.1073/pnas.95.22.12825
https://doi.org/10.1073/pnas.95.22.12825
Autor:
G.R. Moore, Michael J. Osborne, Marcia R. Mauk, Mauk Ag, P D Barker, D. Crowe, Federico I. Rosell, Mark C Cox, Jordi Bujons
Publikováno v:
Biochemical Journal. 332:439-449
The reductively dimethylated derivatives of horse and yeast iso-1-ferricytochromes c have been prepared and characterized for use as NMR probes of the complexes formed by cytochrome c with bovine liver cytochrome b5 and yeast cytochrome c peroxidase.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b52609bcc5679b9d472964c4a383b204
https://doi.org/10.1042/bj3320439
https://doi.org/10.1042/bj3320439
Publikováno v:
Biochemistry. 37:6767-6771
The stability of Mn(II) binding to manganese peroxidase (MnP) has been studied as a function of pH by spectrophotometric and potentiometric titrations. The sensitivity of the potentiometric titrations allows collection of data that are consistent wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d128452ac8840f0fef2769db64cb44c
https://doi.org/10.1021/bi972932u
https://doi.org/10.1021/bi972932u
Publikováno v:
Journal of the American Chemical Society. 119:2146-2155
To characterize the electrostatic complex formed between myoglobin (Mb) and cytochrome b5 (Feb5), we have performed flash photolysis triplet-quenching and electron-transfer (ET) measurements of the...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5cfa4488e10f1d52142d5d2f60e26eb1
https://doi.org/10.1021/ja9630811
https://doi.org/10.1021/ja9630811
Autor:
Mauk Ag, Rafael G. Saer, J.T. Beatty, Michael E. P. Murphy, Federico I. Rosell, Amelia Hardjasa
Publikováno v:
Biochemistry. 52(13)
In the native reaction center (RC) of Rhodobacter sphaeroides, the side chain of (M)L214 projects orthogonally toward the plane and into the center of the A branch bacteriopheophytin (BPhe) macrocycle. The possibility that this side chain is responsi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1e478dc47395043559617305bb2d728
https://pubmed.ncbi.nlm.nih.gov/23480277
https://pubmed.ncbi.nlm.nih.gov/23480277