211 related articles for article (PubMed ID: 23530865)
1. HHM motif at the CuH-site of peptidylglycine monooxygenase is a pH-dependent conformational switch.
Kline CD; Mayfield M; Blackburn NJ
Biochemistry; 2013 Apr; 52(15):2586-96. PubMed ID: 23530865
[TBL] [Abstract][Full Text] [Related]
2. A copper-methionine interaction controls the pH-dependent activation of peptidylglycine monooxygenase.
Bauman AT; Broers BA; Kline CD; Blackburn NJ
Biochemistry; 2011 Dec; 50(50):10819-28. PubMed ID: 22080626
[TBL] [Abstract][Full Text] [Related]
3. Binding of copper and silver to single-site variants of peptidylglycine monooxygenase reveals the structure and chemistry of the individual metal centers.
Chauhan S; Kline CD; Mayfield M; Blackburn NJ
Biochemistry; 2014 Feb; 53(6):1069-80. PubMed ID: 24471980
[TBL] [Abstract][Full Text] [Related]
4. Stopped-Flow Studies of the Reduction of the Copper Centers Suggest a Bifurcated Electron Transfer Pathway in Peptidylglycine Monooxygenase.
Chauhan S; Hosseinzadeh P; Lu Y; Blackburn NJ
Biochemistry; 2016 Apr; 55(13):2008-21. PubMed ID: 26982589
[TBL] [Abstract][Full Text] [Related]
5. Isocyanide binding to the copper(I) centers of the catalytic core of peptidylglycine monooxygenase (PHMcc).
Rhames FC; Murthy NN; Karlin KD; Blackburn NJ
J Biol Inorg Chem; 2001 Jun; 6(5-6):567-77. PubMed ID: 11472020
[TBL] [Abstract][Full Text] [Related]
6. The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase (PHM): a spectroscopic study of the H172A mutant.
Jaron S; Mains RE; Eipper BA; Blackburn NJ
Biochemistry; 2002 Nov; 41(44):13274-82. PubMed ID: 12403629
[TBL] [Abstract][Full Text] [Related]
7. Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Spectroscopic definition of the resting sites and the putative CuIIM-OOH intermediate.
Chen P; Bell J; Eipper BA; Solomon EI
Biochemistry; 2004 May; 43(19):5735-47. PubMed ID: 15134448
[TBL] [Abstract][Full Text] [Related]
8. The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase: a kinetic study of the H172A mutant.
Evans JP; Blackburn NJ; Klinman JP
Biochemistry; 2006 Dec; 45(51):15419-29. PubMed ID: 17176064
[TBL] [Abstract][Full Text] [Related]
9. Substrate-Induced Carbon Monoxide Reactivity Suggests Multiple Enzyme Conformations at the Catalytic Copper M-Center of Peptidylglycine Monooxygenase.
Kline CD; Blackburn NJ
Biochemistry; 2016 Dec; 55(48):6652-6661. PubMed ID: 27933800
[TBL] [Abstract][Full Text] [Related]
10. Does superoxide channel between the copper centers in peptidylglycine monooxygenase? A new mechanism based on carbon monoxide reactivity.
Jaron S; Blackburn NJ
Biochemistry; 1999 Nov; 38(46):15086-96. PubMed ID: 10563791
[TBL] [Abstract][Full Text] [Related]
11. Kβ Valence to Core X-ray Emission Studies of Cu(I) Binding Proteins with Mixed Methionine - Histidine Coordination. Relevance to the Reactivity of the M- and H-sites of Peptidylglycine Monooxygenase.
Martin-Diaconescu V; Chacón KN; Delgado-Jaime MU; Sokaras D; Weng TC; DeBeer S; Blackburn NJ
Inorg Chem; 2016 Apr; 55(7):3431-9. PubMed ID: 26965786
[TBL] [Abstract][Full Text] [Related]
12. Mechanistic investigation of peptidylglycine alpha-hydroxylating monooxygenase via intrinsic tryptophan fluorescence and mutagenesis.
Bell J; El Meskini R; D'Amato D; Mains RE; Eipper BA
Biochemistry; 2003 Jun; 42(23):7133-42. PubMed ID: 12795609
[TBL] [Abstract][Full Text] [Related]
13. Catalytic M Center of Copper Monooxygenases Probed by Rational Design. Effects of Selenomethionine and Histidine Substitution on Structure and Reactivity.
Alwan KB; Welch EF; Blackburn NJ
Biochemistry; 2019 Nov; 58(44):4436-4446. PubMed ID: 31626532
[TBL] [Abstract][Full Text] [Related]
14. Investigation of the pathway for inter-copper electron transfer in peptidylglycine alpha-amidating monooxygenase.
Francisco WA; Wille G; Smith AJ; Merkler DJ; Klinman JP
J Am Chem Soc; 2004 Oct; 126(41):13168-9. PubMed ID: 15479039
[TBL] [Abstract][Full Text] [Related]
15. The catalytic core of peptidylglycine alpha-hydroxylating monooxygenase: investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance.
Eipper BA; Quon AS; Mains RE; Boswell JS; Blackburn NJ
Biochemistry; 1995 Mar; 34(9):2857-65. PubMed ID: 7893699
[TBL] [Abstract][Full Text] [Related]
16. Lumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase.
Otoikhian A; Barry AN; Mayfield M; Nilges M; Huang Y; Lutsenko S; Blackburn NJ
J Am Chem Soc; 2012 Jun; 134(25):10458-68. PubMed ID: 22577880
[TBL] [Abstract][Full Text] [Related]
17. Structural investigations on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine alpha-amidating enzyme.
Boswell JS; Reedy BJ; Kulathila R; Merkler D; Blackburn NJ
Biochemistry; 1996 Sep; 35(38):12241-50. PubMed ID: 8823157
[TBL] [Abstract][Full Text] [Related]
18. The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role.
Siebert X; Eipper BA; Mains RE; Prigge ST; Blackburn NJ; Amzel LM
Biophys J; 2005 Nov; 89(5):3312-9. PubMed ID: 16100265
[TBL] [Abstract][Full Text] [Related]
19. Characterization of a half-apo derivative of peptidylglycine monooxygenase. Insight into the reactivity of each active site copper.
Jaron S; Blackburn NJ
Biochemistry; 2001 Jun; 40(23):6867-75. PubMed ID: 11389601
[TBL] [Abstract][Full Text] [Related]
20. The copper centers of tyramine β-monooxygenase and its catalytic-site methionine variants: an X-ray absorption study.
Hess CR; Klinman JP; Blackburn NJ
J Biol Inorg Chem; 2010 Nov; 15(8):1195-207. PubMed ID: 20544364
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]