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01000naa a22002652 4500 |
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NLM117963291 |
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DE-627 |
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20231222181648.0 |
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231222s2002 xx ||||| 00| ||eng c |
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|a pubmed24n0393.xml
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|a (DE-627)NLM117963291
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|a (NLM)11913390
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Torrent, Maricel
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Computational studies of reaction mechanisms of methane monooxygenase and ribonucleotide reductase
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| 264 |
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|c 2002
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 22.05.2002
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|a Date Revised 21.11.2013
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|a published: Print
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|a Citation Status MEDLINE
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|a An overview of the computational efforts made by our group during the last few years in the field of nonheme diiron proteins is presented. Through application of ab initio methodology to a reasonable set of molecular models, significant progress is made in understanding how the soluble Methane Monooxygenase system achieves the hydroxylation of methane and how the catalytic cycle of Ribonucleotide Reductase is initiated. In particular, the current studies reveal in more detail (1) the nature of key intermediates in the reaction cycles of these two metalloenzymes, (2) details of how the iron centers regulate the systems, and (3) important aspects of how the carboxylate ligands in the active sites may tailor the enzymatic needs of the metalloprotein. This knowledge also leads to novel connections between the two enzymes. The coordinative unsaturation and carboxylate shifts investigated herein are two properties that are likely to be of more general impact in nonheme proteins. The control of the redox chemistry of the enzyme by the binuclear metal center, also analyzed here, should find common ground among other bimetallic systems as well
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| 650 |
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|a Comparative Study
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| 650 |
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|a Journal Article
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| 650 |
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|a Research Support, Non-U.S. Gov't
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| 650 |
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 650 |
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7 |
|a Metalloproteins
|2 NLM
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| 650 |
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|a Nonheme Iron Proteins
|2 NLM
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| 650 |
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|a Water
|2 NLM
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| 650 |
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|a 059QF0KO0R
|2 NLM
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| 650 |
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|a Iron
|2 NLM
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| 650 |
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7 |
|a E1UOL152H7
|2 NLM
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| 650 |
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|a Oxygenases
|2 NLM
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| 650 |
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|a EC 1.13.-
|2 NLM
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| 650 |
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|a methane monooxygenase
|2 NLM
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| 650 |
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|a EC 1.14.13.25
|2 NLM
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| 650 |
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|a Ribonucleotide Reductases
|2 NLM
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| 650 |
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7 |
|a EC 1.17.4.-
|2 NLM
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| 700 |
1 |
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|a Musaev, Djamaladdin G
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Basch, Harold
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Morokuma, Keiji
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of computational chemistry
|d 1984
|g 23(2002), 1 vom: 15. Jan., Seite 59-76
|w (DE-627)NLM098138448
|x 1096-987X
|7 nnns
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| 773 |
1 |
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|g volume:23
|g year:2002
|g number:1
|g day:15
|g month:01
|g pages:59-76
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|a AR
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|d 23
|j 2002
|e 1
|b 15
|c 01
|h 59-76
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