Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Yergalem T. Meharenna"'
Autor:
Yergalem T. Meharenna, S. Michael Soltis, S.E. McPhillips, J. Song, E.L. Baxter, Georges Chreifi, Aina E. Cohen, Tzanko Doukov, Thomas L. Poulos
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 113, iss 5
The reaction of peroxides with peroxidases oxidizes the heme iron from Fe(III) to Fe(IV)=O and a porphyrin or aromatic side chain to a cationic radical. X-ray-generated hydrated electrons rapidly reduce Fe(IV), thereby requiring very short exposures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09e90fd8b5d21b1bf555234dd43988c1
https://doi.org/10.1073/pnas.1521664113
https://doi.org/10.1073/pnas.1521664113
Autor:
Lyndal M. R. Jensen, Thomas L. Poulos, Carrie M. Wilmot, Ritimukta Sarangi, Britt Hedman, Yergalem T. Meharenna, Victor L. Davidson
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 17:1241-1255
Biosynthesis of the tryptophan tryptophylquinone (TTQ) cofactor activates the enzyme methylamine dehydrogenase. The diheme enzyme MauG catalyzes O-atom insertion and cross-linking of two Trp residues to complete TTQ synthesis. Solution optical and M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96ab967576fc4682d22367b7359bc334
https://doi.org/10.1007/s00775-012-0939-3
https://doi.org/10.1007/s00775-012-0939-3
Publikováno v:
Biochemistry. 49:6680-6686
High-temperature molecular dynamics (MD) has been used to assess if MD can be employed as a useful tool for probing the structural basis for enhanced stability in thermal stable cytochromes P450. CYP119, the most thermal stable P450 known, unfolds mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e04adc0fb908df8daab82228235eef3
https://doi.org/10.1021/bi100929x
https://doi.org/10.1021/bi100929x
Publikováno v:
Biochemistry. 48:5839-5848
DevS is one of the two sensing kinases responsible for DevR activation and the subsequent entry of Mycobacterium tuberculosis into dormancy. Full length wild-type DevS forms a stable oxy-ferrous complex. The DevS autooxidation rates are extremely low
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0658b97087cac3ad901cf43d858177e7
https://doi.org/10.1021/bi802309y
https://doi.org/10.1021/bi802309y
Publikováno v:
Biochemistry. 47:10324-10332
Cytochrome c peroxidase (CCP) and ascorbate peroxidase (APX) have very similar structures, and yet neither CCP nor APX exhibits each other's activities with respect to reducing substrates. APX has a unique substrate binding site near the heme propion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::175f2df53c37107b9b1a11a61bf66f7e
https://doi.org/10.1021/bi8007565
https://doi.org/10.1021/bi8007565
Autor:
Thomas L. Poulos, Yergalem T. Meharenna, Kate E. Slessor, James J. De Voss, Sonia M. Cavaignac
Publikováno v:
Journal of Biological Chemistry. 283:10804-10812
Cytochrome P450cin (CYP176A1) is a bacterial P450 isolated from Citrobacter braakii that catalyzes the hydroxylation of cineole to (S)-6β-hydroxycineole. This initiates the biodegradation of cineole, enabling C. braakii to live on cineole as its sol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db9e9692cc47a592d5347ef7fc88a519
https://doi.org/10.1074/jbc.m709722200
https://doi.org/10.1074/jbc.m709722200
Autor:
Stephen G. Sligar, Aditi Das, Yergalem T. Meharenna, Novelle Kimmich, Irina F. Sevrioukova, Thomas L. Poulos
Publikováno v:
Journal of Biological Chemistry. 282:27006-27011
Cytochrome P450 reductase, which delivers electrons from NADPH to microsomal P450s, consists of a single polypeptide that contains both FAD and FMN. The bacterial P450cin utilizes a similar electron transport system except the FAD/FMN reductase consi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8d12e14882cd8b44846435c0f87de7b
https://doi.org/10.1074/jbc.m703790200
https://doi.org/10.1074/jbc.m703790200
Publikováno v:
Journal of Biological Chemistry. 282:1066-1071
Heme oxygenases have an increased binding affinity for O2 relative to CO. Such discrimination is critical to the function of HO enzymes because one of the main products of heme catabolism is CO. Kinetic studies of mammalian and bacterial HO proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86404bcc632b283a64c59ecf8ed51101
https://doi.org/10.1074/jbc.m609112200
https://doi.org/10.1074/jbc.m609112200
Autor:
James J. De Voss, David B. Hawkes, Yergalem T. Meharenna, Thomas L. Poulos, H. Li, Andrew G. Pearson
Publikováno v:
Biochemistry. 43:9487-9494
Cytochrome P450cin catalyzes the monooxygenation of 1,8-cineole, which is structurally very similar to D-camphor, the substrate for the most thoroughly investigated cytochrome P450, cytochrome P450cam. Both 1,8-cineole and D-camphor are C-10 monoterp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2be47bd757ebdd79b60af709b518ef32
https://doi.org/10.1021/bi049293p
https://doi.org/10.1021/bi049293p
Autor:
Sheila J. Sadeghi, Gianfranco Gilardi, Yergalem T. Meharenna, Silva Giannini, Michael Fairhead, Georgia Eleni Tsotsou
Publikováno v:
Biosensors and Bioelectronics. 17:133-145
This paper reports on the application of the molecular Lego approach to P450 enzymes. Protein domains are used as catalytic (P450 BM3 haem domain and human P450 2E1) or electron transfer (flavodoxin and P450 BM3 reductase) modules. The objectives are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe0dbae7a9c167efa094b6be822bd57f
https://doi.org/10.1016/s0956-5663(01)00286-x
https://doi.org/10.1016/s0956-5663(01)00286-x