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Abstract:

Many bioactive peptides, such as hormones and neuropeptides, require amidation at the C terminus for their full biological activity. Peptidylglycine α-hydroxylating monooxygenase (PHM) performs the first step of the amidation reaction - the hydroxylation of peptidylglycine substrates at the Cα position of the terminal glycine. The hydroxylation reaction is copper- and O2-dependent and requires 2 equiv of exogenous reductant. The proposed mechanism suggests that O2 is reduced by two electrons, each provided by one of two nonequivalent copper sites in PHM (CuH and CuM). The characteristics of the reduced oxygen species in the PHM reaction and the identity of the reactive intermediate remain uncertain. To further investigate the nature of the key intermediates in the PHM cycle, we determined the structure of the oxidized form of PHM complexed with hydrogen peroxide. In this 1.98-Å-resolution structure (hydro)peroxide binds solely to CuM in a slightly asymmetric side-on mode. The O-O interatomic distance of the copper-bound ligand is 1.5 Å, characteristic of peroxide/hydroperoxide species, and the Cu-O distances are 2.0 and 2.1 Å. Density functional theory calculations using the first coordination sphere of the CuM active site as a model system show that the computed energies of the side-on L3CuM(II)-O2 2- species and its isomeric, end-on structure L3CuM(I)-O 2 ·- are similar, suggesting that both these intermediates are significantly populated within the protein environment. This observation has important mechanistic implications. The geometry of the observed side-on coordinated peroxide ligand in L3CuM(II)O 2 2- is in good agreement with the results of a hybrid quantum mechanical-molecular mechanical optimization of this species. © 2012 SBIC.

Registro:

Documento: Artículo
Título:Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): Structural and computational study
Autor:Rudzka, K.; Moreno, D.M.; Eipper, B.; Mains, R.; Estrin, D.A.; Amzel, L.M.
Filiación:Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Johns Hopkins University, Baltimore, MD 21205, United States
Department of Inorganic, Analytical and Physical Chemistry, University of Buenos Aires, Buenos Aires, Argentina
Department of Neuroscience and Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, United States
Palabras clave:Amidation of peptides; Copper-containing proteins; Peptidylglycine α-hydroxylating monooxygenase; Peroxide; copper H; copper ion; copper M; cupric ion; cuprous ion; glycine; hydrogen peroxide; oxygen derivative; oxygenase; peptidylglycine alpha hydroxylating monooxygenase; peroxide; unclassified drug; amidation; animal cell; article; carboxy terminal sequence; catalysis; complex formation; controlled study; crystal structure; energy; enzyme active site; enzyme binding; enzyme metabolism; female; hamster; hydroxylation; isomer; ligand binding; molecular interaction; molecular mechanics; molecular model; nonhuman; priority journal; quantum mechanics; structure activity relation; structure analysis; X ray diffraction; Animals; Catalytic Domain; CHO Cells; Computer Simulation; Coordination Complexes; Copper; Cricetinae; Crystallography, X-Ray; Hydrogen Bonding; Hydrogen Peroxide; Mixed Function Oxygenases; Models, Molecular; Multienzyme Complexes; Quantum Theory; Rats
Año:2013
Volumen:18
Número:2
Página de inicio:223
Página de fin:232
DOI: http://dx.doi.org/10.1007/s00775-012-0967-z
Título revista:Journal of Biological Inorganic Chemistry
Título revista abreviado:J. Biol. Inorg. Chem.
ISSN:09498257
CODEN:JJBCF
CAS:glycine, 56-40-6, 6000-43-7, 6000-44-8; hydrogen peroxide, 7722-84-1; oxygenase, 9037-29-0, 9046-59-7; peroxide, 14915-07-2; Coordination Complexes; Copper, 7440-50-8; Hydrogen Peroxide, 7722-84-1; Mixed Function Oxygenases, 1.-; Multienzyme Complexes; peptidylglycine monooxygenase, 1.14.17.3
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09498257_v18_n2_p223_Rudzka

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Citas:

---------- APA ----------
Rudzka, K., Moreno, D.M., Eipper, B., Mains, R., Estrin, D.A. & Amzel, L.M. (2013) . Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): Structural and computational study. Journal of Biological Inorganic Chemistry, 18(2), 223-232.
http://dx.doi.org/10.1007/s00775-012-0967-z
---------- CHICAGO ----------
Rudzka, K., Moreno, D.M., Eipper, B., Mains, R., Estrin, D.A., Amzel, L.M. "Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): Structural and computational study" . Journal of Biological Inorganic Chemistry 18, no. 2 (2013) : 223-232.
http://dx.doi.org/10.1007/s00775-012-0967-z
---------- MLA ----------
Rudzka, K., Moreno, D.M., Eipper, B., Mains, R., Estrin, D.A., Amzel, L.M. "Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): Structural and computational study" . Journal of Biological Inorganic Chemistry, vol. 18, no. 2, 2013, pp. 223-232.
http://dx.doi.org/10.1007/s00775-012-0967-z
---------- VANCOUVER ----------
Rudzka, K., Moreno, D.M., Eipper, B., Mains, R., Estrin, D.A., Amzel, L.M. Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): Structural and computational study. J. Biol. Inorg. Chem. 2013;18(2):223-232.
http://dx.doi.org/10.1007/s00775-012-0967-z