Literature summary for 1.14.17.3 extracted from

Martin-Diaconescu, V.; Chacon, K.N.; Delgado-Jaime, M.U.; Sokaras, D.; Weng, T.C.; DeBeer, S.; Blackburn, N.J.
Kbeta 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 (2016), Inorg. Chem., 55, 3431-3439 .

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Protein Variants

Protein Variants	Comment	Organism
H107A/H108A	site-directed mutagenesis, structure analysis of copper centers compared to wild-type	Rattus norvegicus
H242A	site-directed mutagenesis, structure analysis of copper centers compared to wild-type	Rattus norvegicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	two distinct Cu centers are located in the protein active site. Of the two distinct Cu centers in the protein active site (separated by 11 A), the CuH site, believed to serve primarily as an electron transfer site, is coordinated by three histidines, H107, H108, H172, in a roughly T-shaped geometry. The CuM site, where oxygen binding and hydroxylation occur, has a mixed coordination sphere consisting of two histidines, H242, and H244, and a methionine, M314. Reaction mechanism, overview. Reaction of wild-type enzyme PHM with CO (an oxygen analogue) produces the M-site CO complex, which shows a unique XES spectrum that can be computationally reproduced by including interactions between Cu(I) and the CO ligand. The valence-to-core (VtC) region can serve as a probe of not only ligand speciation, but also offer insight into the coordination geometry, in a fashion similar to XAS pre-edges, and may be sufficiently sensitive to the coordination of exogenous ligands to be useful in the study of reaction mechanisms. Application of X-ray emission spectroscopy to copper proteins via a study of a series of mixed His-Met copper sites where the ligand set varies in a systematic way between the His3 and Met3 limits. The sites are derived from the wild-type peptidylglycine monooxygenase (PHM), two single-site variants which replicate each of its two copper sites (CuM-site and CuH-site), and the transporters CusF and CusB. Structure analysis of copper centers of wild-type and mutant enzymes	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P14925	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	peptidylglycine alpha-hydroxylating monooxygenase (PHM) catalyzes stereospecific alpha-C hydroxylation of C-terminal glycines, the first step in the alpha-amidation of hormones, growth factors and neurotransmitters. The molecular oxygen-dependent reaction requires two equivalents of ascorbate as exogenous reductant, releasing water and semidehydroascorbate as byproducts	Rattus norvegicus	?	-	?

Synonyms

Synonyms	Comment	Organism
PHM	-	Rattus norvegicus

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Release 2023.1 (January 2023)