123 related articles for article (PubMed ID: 30696768)
1. The reactive form of a C-S bond-cleaving, CO
Streit BR; Mattice JR; Prussia GA; Peters JW; DuBois JL
J Biol Chem; 2019 Mar; 294(13):5137-5145. PubMed ID: 30696768
[TBL] [Abstract][Full Text] [Related]
2. Roles of the redox-active disulfide and histidine residues forming a catalytic dyad in reactions catalyzed by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.
Kofoed MA; Wampler DA; Pandey AS; Peters JW; Ensign SA
J Bacteriol; 2011 Sep; 193(18):4904-13. PubMed ID: 21764916
[TBL] [Abstract][Full Text] [Related]
3. The unique Phe-His dyad of 2-ketopropyl coenzyme M oxidoreductase/carboxylase selectively promotes carboxylation and S-C bond cleavage.
Prussia GA; Shisler KA; Zadvornyy OA; Streit BR; DuBois JL; Peters JW
J Biol Chem; 2021 Aug; 297(2):100961. PubMed ID: 34265301
[TBL] [Abstract][Full Text] [Related]
4. Substitution of a conserved catalytic dyad into 2-KPCC causes loss of carboxylation activity.
Prussia GA; Gauss GH; Mus F; Conner L; DuBois JL; Peters JW
FEBS Lett; 2016 Sep; 590(17):2991-6. PubMed ID: 27447465
[TBL] [Abstract][Full Text] [Related]
5. Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Nocek B; Jang SB; Jeong MS; Clark DD; Ensign SA; Peters JW
Biochemistry; 2002 Oct; 41(43):12907-13. PubMed ID: 12390015
[TBL] [Abstract][Full Text] [Related]
6. Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system.
Clark DD; Allen JR; Ensign SA
Biochemistry; 2000 Feb; 39(6):1294-304. PubMed ID: 10684609
[TBL] [Abstract][Full Text] [Related]
7. A catalytic dyad modulates conformational change in the CO
Mattice JR; Shisler KA; DuBois JL; Peters JW; Bothner B
J Biol Chem; 2022 May; 298(5):101884. PubMed ID: 35367206
[TBL] [Abstract][Full Text] [Related]
8. Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.
Pandey AS; Mulder DW; Ensign SA; Peters JW
FEBS Lett; 2011 Feb; 585(3):459-64. PubMed ID: 21192936
[TBL] [Abstract][Full Text] [Related]
9. Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Pandey AS; Nocek B; Clark DD; Ensign SA; Peters JW
Biochemistry; 2006 Jan; 45(1):113-20. PubMed ID: 16388586
[TBL] [Abstract][Full Text] [Related]
10. Mechanism of inhibition of aliphatic epoxide carboxylation by the coenzyme M analog 2-bromoethanesulfonate.
Boyd JM; Clark DD; Kofoed MA; Ensign SA
J Biol Chem; 2010 Aug; 285(33):25232-42. PubMed ID: 20551308
[TBL] [Abstract][Full Text] [Related]
11. Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Jang SB; Jeong MS; Clark DD; Ensign SA; Peters JW
Acta Crystallogr D Biol Crystallogr; 2001 Mar; 57(Pt 3):445-7. PubMed ID: 11223527
[TBL] [Abstract][Full Text] [Related]
12. Purification and characterization of a flavoprotein involved in the degradation of epoxyalkanes by Xanthobacter Py2.
Westphal AH; Swaving J; Jacobs L; De Kok A
Eur J Biochem; 1998 Oct; 257(1):160-8. PubMed ID: 9799115
[TBL] [Abstract][Full Text] [Related]
13. Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli.
Rietveld P; Arscott LD; Berry A; Scrutton NS; Deonarain MP; Perham RN; Williams CH
Biochemistry; 1994 Nov; 33(46):13888-95. PubMed ID: 7947797
[TBL] [Abstract][Full Text] [Related]
14. Characterization of 2-bromoethanesulfonate as a selective inhibitor of the coenzyme m-dependent pathway and enzymes of bacterial aliphatic epoxide metabolism.
Boyd JM; Ellsworth A; Ensign SA
J Bacteriol; 2006 Dec; 188(23):8062-9. PubMed ID: 16997966
[TBL] [Abstract][Full Text] [Related]
15. A hydrogen bond network in the active site of Anabaena ferredoxin-NADP(+) reductase modulates its catalytic efficiency.
Sánchez-Azqueta A; Herguedas B; Hurtado-Guerrero R; Hervás M; Navarro JA; Martínez-Júlvez M; Medina M
Biochim Biophys Acta; 2014 Feb; 1837(2):251-63. PubMed ID: 24200908
[TBL] [Abstract][Full Text] [Related]
16. Electron transfer in flavocytochrome P450 BM3: kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase.
Roitel O; Scrutton NS; Munro AW
Biochemistry; 2003 Sep; 42(36):10809-21. PubMed ID: 12962506
[TBL] [Abstract][Full Text] [Related]
17. Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry.
Distefano MD; Au KG; Walsh CT
Biochemistry; 1989 Feb; 28(3):1168-83. PubMed ID: 2653436
[TBL] [Abstract][Full Text] [Related]
18. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis.
Waksman G; Krishna TS; Williams CH; Kuriyan J
J Mol Biol; 1994 Feb; 236(3):800-16. PubMed ID: 8114095
[TBL] [Abstract][Full Text] [Related]
19. Reductive half-reaction of thioredoxin reductase from Escherichia coli.
Lennon BW; Williams CH
Biochemistry; 1997 Aug; 36(31):9464-77. PubMed ID: 9235991
[TBL] [Abstract][Full Text] [Related]
20. Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases.
Gutierrez A; Doehr O; Paine M; Wolf CR; Scrutton NS; Roberts GC
Biochemistry; 2000 Dec; 39(51):15990-9. PubMed ID: 11123926
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]