A radical intermediate in tyrosine scission to the CO and CN- ligands of FeFe hydrogenase.
about
Catalytic Promiscuity of the Radical S-adenosyl-L-methionine Enzyme NosLSpore photoproduct lyase: the known, the controversial, and the unknownCrystal structure of HydG from Carboxydothermus hydrogenoformans: a trifunctional [FeFe]-hydrogenase maturaseThe drive to life on wet and icy worldsA Redox Active [2Fe-2S] Cluster on the Hydrogenase Maturase HydF.Paramagnetic intermediates generated by radical S-adenosylmethionine (SAM) enzymesThe cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster.Recent advances in radical SAM enzymology: new structures and mechanisms.Reversible H atom abstraction catalyzed by the radical S-adenosylmethionine enzyme HydG.X-ray crystallographic and EPR spectroscopic analysis of HydG, a maturase in [FeFe]-hydrogenase H-cluster assembly.Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM)Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl radicals in deazaflavin biosynthesisThe HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster.Cysteine as a ligand platform in the biosynthesis of the FeFe hydrogenase H cluster.EPR Spectroscopic Studies of [FeFe]-Hydrogenase Maturation.CO and CN- syntheses by [FeFe]-hydrogenase maturase HydG are catalytically differentiated events.The Radical SAM Enzyme HydG Requires Cysteine and a Dangler Iron for Generating an Organometallic Precursor to the [FeFe]-Hydrogenase H-ClusterBiosynthesis of the [FeFe] Hydrogenase H Cluster: A Central Role for the Radical SAM Enzyme HydG[FeFe]-hydrogenase maturation: insights into the role HydE plays in dithiomethylamine biosynthesis.Radical S-adenosylmethionine enzymes.H-cluster assembly during maturation of the [FeFe]-hydrogenase.Radical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.Rapid Freeze-Quench EPR Spectroscopy: Improved Collection of Frozen Particles.Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation.Cell-free protein synthesis enables high yielding synthesis of an active multicopper oxidase.Reactivity of the nitrogen-centered tryptophanyl radical in the catalysis by the radical SAM enzyme NosL.Mechanistic Insights into the Radical S-adenosyl-l-methionine Enzyme NosL From a Substrate Analogue and the Shunt Products.Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions.Fine-tuning of a radical-based reaction by radical S-adenosyl-L-methionine tryptophan lyase.Cross-Polarization Electron-Nuclear Double Resonance Spectroscopy.
P2860
Q26742087-3BA51E8D-1DE3-4668-B337-0C467C851D99Q26863308-B76D6912-3563-402B-945B-B1BBF2D6EBA9Q27696855-448F461F-C41E-4528-9C9F-A00957854FDFQ28658605-796F184D-649B-40BC-9CE2-AFEBE98DDB30Q33885103-02E0114D-0D96-4A04-8C37-637667F2856DQ34070183-2EEF2D88-B03B-4842-ABBB-7ED6DCD5DABAQ34145210-9099F01B-16EE-43BB-A8B1-1EA610B0080CQ34211575-E22F06DF-C416-4816-8FCB-2266567D492EQ34282694-14640870-05D9-41AA-87AE-2E2ABAE710D2Q35062774-1D96A895-DB21-4B5C-8ABE-33FCAC9A428BQ35329323-C94FE6EE-6A79-4BA3-92B2-A810D1AFF471Q35559263-F24CC455-4675-4FD2-82FE-4CB38094A81CQ35886414-F243C8FA-B54C-46D2-87D3-5334E78BA36AQ36079128-7928BC36-CFE7-43FB-84A3-F8D8F66CCA65Q36200898-8F01BEFD-934A-43C6-86A8-BD2831AB39E1Q36459485-405D4075-8022-41ED-B06F-0CC9D432AF92Q36635298-884E7B27-4CEA-4A0A-90FC-D0C65331937CQ36659198-164992CB-E0C7-49A5-8973-7D8D9ECCF606Q36820707-CE80A511-B569-4FE7-8AE7-6F6C052F1C8AQ37727698-B816BEA7-3912-4104-A11D-3AD53BE0EF88Q38223922-16243040-2621-4AD8-806B-316AF3A333CBQ38283509-8ABECC6C-B5A1-45A8-A6A8-A500378A4B47Q42772519-6807749A-094A-4B66-9602-9347E37E68B6Q46363546-6950A17D-D2A4-4177-9BA3-F61430175C58Q46476715-DE554788-27DA-4646-A971-D61950501B81Q48174934-2EDA7D82-A53E-4982-8B28-324FACD2548FQ48248930-6E5CDF89-EE30-4F1F-8455-E3ACB0BFA54DQ51215367-42191A8B-E90A-46A1-BFEB-648732475818Q52669486-C6D0E20F-F406-4DE8-884C-BCF82EB2A42CQ54258172-A346DD54-68D0-46FE-A3B0-0690CCCBBC71
P2860
A radical intermediate in tyrosine scission to the CO and CN- ligands of FeFe hydrogenase.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh
2013年學術文章
@zh-hant
name
A radical intermediate in tyro ...... - ligands of FeFe hydrogenase.
@en
A radical intermediate in tyro ...... - ligands of FeFe hydrogenase.
@nl
type
label
A radical intermediate in tyro ...... - ligands of FeFe hydrogenase.
@en
A radical intermediate in tyro ...... - ligands of FeFe hydrogenase.
@nl
prefLabel
A radical intermediate in tyro ...... - ligands of FeFe hydrogenase.
@en
A radical intermediate in tyro ...... - ligands of FeFe hydrogenase.
@nl
P2093
P2860
P356
P1433
P1476
A radical intermediate in tyrosine scission to the CO and CN- ligands of FeFe hydrogenase
@en
P2093
James R Swartz
Jon M Kuchenreuther
R David Britt
Simon J George
Troy A Stich
P2860
P304
P356
10.1126/SCIENCE.1241859
P407
P577
2013-10-01T00:00:00Z