The catalytic mechanism of peptidylglycine α-hydroxylating monooxygenase investigated by computer simulation

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The molecular basis of the hydroxylation reaction of the Cα of a C-terminal glycine catalyzed by peptidylglycine α-hydroxylating monooxygenase (PHM) was investigated using hybrid quantum-classical (QM-MM) computational techniques. We have identified the most reactive oxygenated species and presented...

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Autor principal: Crespo, A.
Otros Autores: Martí, M.A, Roitberg, A.E, Amzel, L.M, Estrin, D.A
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2006
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-33749526867 
024 7 |2 cas  |a ascorbic acid, 134-03-2, 15421-15-5, 50-81-7; cytochrome P450, 9035-51-2; glycine, 56-40-6, 6000-43-7, 6000-44-8; hydrogen, 12385-13-6, 1333-74-0; proton, 12408-02-5, 12586-59-3; unspecific monooxygenase, 9012-80-0, 9037-52-9, 9038-14-6; Hydrogen, 1333-74-0; Mixed Function Oxygenases, 1.-; Multienzyme Complexes; Oxygen, 7782-44-7; peptidylglycine monooxygenase, 1.14.17.3 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a JACSA 
100 1 |a Crespo, A. 
245 1 4 |a The catalytic mechanism of peptidylglycine α-hydroxylating monooxygenase investigated by computer simulation 
260 |c 2006 
270 1 0 |m Amzel, L.M.; Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States; email: mario@neruda.med.jhmi.edu 
506 |2 openaire  |e Política editorial 
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520 3 |a The molecular basis of the hydroxylation reaction of the Cα of a C-terminal glycine catalyzed by peptidylglycine α-hydroxylating monooxygenase (PHM) was investigated using hybrid quantum-classical (QM-MM) computational techniques. We have identified the most reactive oxygenated species and presented new insights into the hydrogen abstraction (H-abstraction) mechanism operative in PHM. Our results suggest that O2 binds to CuB to generate CuB II-O2 .- followed by electron transfer (ET) from CuA to form CuB I-O2 .-. The computed potential energy profiles for the H-abstraction reaction for CuB II-O2 .-, CuB I-O 2 ., and [CuB II-OOH]+ species indicate that none of these species can be responsible for abstraction. However, the latter species can spontaneously form [CuBO] +2 (which consists of a two-unpaired-electrons [CuBO] + moiety ferromagneticaly coupled with a radical cation located over the three CuB ligands, in the quartet spin ground state) by abstracting a proton from the surrounding solvent. Both this monooxygenated species and the one obtained by reduction with ascorbate, [CuBO] +, were found to be capable of carrying out the H-abstraction; however, whereas the former abstracts the hydrogen atom concertedly with almost no activation energy, the later forms an intermediate that continues the reaction by a rebinding step. We propose that the active species in H-abstraction in PHM is probably [CuBO]+2 because it is formed exothermically and can concertedly abstract the substrate HA atom with the lower overall activation energy. Interestingly, this species resembles the active oxidant in cytochrome P450 enzymes, Compound I, suggesting that both PHM and cytochrome P450 enzymes may carry out substrate hydroxylation by using a similar mechanism. © 2006 American Chemical Society.  |l eng 
593 |a Departamento de Quimica Inorganica, Analitica y Quimica-Fisica, INQUIMAE-CONICET, Universidad de Buenos Aires, C1428EHA Buenos Aires, Argentina 
593 |a Quantum Theory Project, Department of Chemistry, University of Florida, Gainesville, FL 32611-8435, United States 
593 |a Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States 
690 1 0 |a CYTOCHROME P450 ENZYMES 
690 1 0 |a ELECTRON TRANSFER (ET) 
690 1 0 |a PEPTIDYLGLYCINE Α-HYDROXYLATING MONOOXYGENASE (PHM) 
690 1 0 |a QUANTUM-CLASSICAL (QM-MM) 
690 1 0 |a ACTIVATION ENERGY 
690 1 0 |a CATALYSTS 
690 1 0 |a COMPUTER SIMULATION 
690 1 0 |a GROUND STATE 
690 1 0 |a HYDROXYLATION 
690 1 0 |a POSITIVE IONS 
690 1 0 |a PROTEINS 
690 1 0 |a QUANTUM THEORY 
690 1 0 |a GLYCEROL 
690 1 0 |a ASCORBIC ACID 
690 1 0 |a CYTOCHROME P450 
690 1 0 |a GLYCINE 
690 1 0 |a HYDROGEN 
690 1 0 |a PEPTIDYLGLYCINE ALPHA HYDROXYLATING MONOOXYGENASE 
690 1 0 |a PROTON 
690 1 0 |a REACTIVE OXYGEN METABOLITE 
690 1 0 |a SOLVENT 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a UNSPECIFIC MONOOXYGENASE 
690 1 0 |a ARTICLE 
690 1 0 |a CARBOXY TERMINAL SEQUENCE 
690 1 0 |a CATALYSIS 
690 1 0 |a CHEMICAL BINDING 
690 1 0 |a COMPUTER SIMULATION 
690 1 0 |a ELECTRON TRANSPORT 
690 1 0 |a ENERGY 
690 1 0 |a ENTHALPY 
690 1 0 |a HYDROXYLATION 
690 1 0 |a QUANTUM MECHANICS 
690 1 0 |a REDUCTION 
690 1 0 |a CATALYSIS 
690 1 0 |a COMPUTER SIMULATION 
690 1 0 |a HYDROGEN 
690 1 0 |a HYDROXYLATION 
690 1 0 |a KINETICS 
690 1 0 |a MIXED FUNCTION OXYGENASES 
690 1 0 |a MODELS, MOLECULAR 
690 1 0 |a MULTIENZYME COMPLEXES 
690 1 0 |a OXYGEN 
690 1 0 |a QUANTUM THEORY 
690 1 0 |a THERMODYNAMICS 
700 1 |a Martí, M.A. 
700 1 |a Roitberg, A.E. 
700 1 |a Amzel, L.M. 
700 1 |a Estrin, D.A. 
773 0 |d 2006  |g v. 128  |h pp. 12817-12828  |k n. 39  |p J. Am. Chem. Soc.  |x 00027863  |w (AR-BaUEN)CENRE-19  |t Journal of the American Chemical Society 
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856 4 0 |u https://doi.org/10.1021/ja062876x  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00027863_v128_n39_p12817_Crespo  |y Handle 
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963 |a VARI 
999 |c 82693 

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