„Methan-Monooxygenase“ – Versionsunterschied
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== Literatur == |
== Literatur == |
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* Murrell JC, Lidstrom ME, Holmes AJ, Costello A (1995). "Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related". FEMS Microbiol. Lett. 132 (3): 203–208. doi |
* Murrell JC, Lidstrom ME, Holmes AJ, Costello A (1995). "Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related". FEMS Microbiol. Lett. 132 (3): 203–208. {{doi|10.1111/j.1574-6968.1995.tb07834.x}}. PMID 7590173. |
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* Sayavedra-soto LA, Hommes NG, Arp DJ (2002). "Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea". Arch. Microbiol. 178 (4): 250–255. doi |
* Sayavedra-soto LA, Hommes NG, Arp DJ (2002). "Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea". Arch. Microbiol. 178 (4): 250–255. {{doi|10.1007/s00203-002-0452-0}}. PMID 12209257. |
||
* Lieberman RL, Rosenzweig AC (2005). "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane". Nature 434 (7030): 177–182. {{DOI|10.1038/nature03311}}. PMID 15674245. |
* Lieberman RL, Rosenzweig AC (2005). "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane". Nature 434 (7030): 177–182. {{DOI|10.1038/nature03311}}. PMID 15674245. |
||
* Rosenzweig et al.; Frederick, CA; Lippard, SJ; Nordlund, P (1993). "Crystal structure of bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane". Nature 366 (6455): 537–543. {{DOI|10.1038/366537a0}}. PMID 8255292. |
* Rosenzweig et al.; Frederick, CA; Lippard, SJ; Nordlund, P (1993). "Crystal structure of bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane". Nature 366 (6455): 537–543. {{DOI|10.1038/366537a0}}. PMID 8255292. |
||
* Basch, Harold et al. (1999). "Mechanism of the Methane -> Methanol Conversion Reaction Catalyzed by Methane Monooxygenase: A Density Function Study". J. Am. Chem. Soc. 121 (31): 7249–7256. doi |
* Basch, Harold et al. (1999). "Mechanism of the Methane -> Methanol Conversion Reaction Catalyzed by Methane Monooxygenase: A Density Function Study". J. Am. Chem. Soc. 121 (31): 7249–7256. {{doi|10.1021/ja9906296}}. |
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* Nordlund et al.; Sjöberg, BM; Eklund, H (1990). "Three-dimensional structure of the free radical protein of ribonucleotide reductase". Nature 345 (6276): 593–598. {{DOI|10.1038/345593a0}}. PMID 2190093. |
* Nordlund et al.; Sjöberg, BM; Eklund, H (1990). "Three-dimensional structure of the free radical protein of ribonucleotide reductase". Nature 345 (6276): 593–598. {{DOI|10.1038/345593a0}}. PMID 2190093. |
||
* Nordlund et al.; Eklund, H (1993). "Structure and function of the Escherichia coli ribonucleotide reductase protein R2". J. Mol. Biol. 232 (1): 123–164. {{DOI|10.1006/jmbi.1993.1374}}. PMID 8331655. |
* Nordlund et al.; Eklund, H (1993). "Structure and function of the Escherichia coli ribonucleotide reductase protein R2". J. Mol. Biol. 232 (1): 123–164. {{DOI|10.1006/jmbi.1993.1374}}. PMID 8331655. |
||
* Liu, K et al. (1995). "Characterization of a Diiron(III) Peroxide Intermediate in the Reaction Cycle of Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath)". J. Am. Chem. Soc 117: 4997. doi |
* Liu, K et al. (1995). "Characterization of a Diiron(III) Peroxide Intermediate in the Reaction Cycle of Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath)". J. Am. Chem. Soc 117: 4997. {{doi|10.1021/ja00122a032}}. |
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== Einzelnachweise == |
== Einzelnachweise == |
Version vom 31. Januar 2015, 15:10 Uhr
Methan-Monooxygenase (Methylococcus capsulatus) | ||
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Masse/Länge Primärstruktur | 1677 = (527+388+170) + 141 + 348 + 103 Aminosäuren | |
Sekundär- bis Quartärstruktur | Heterohexamer A(α+β+γ) + B + C + D | |
Kofaktor | Aα: Fe C: (2Fe+2S), FAD | |
Bezeichner | ||
Gen-Name(n) | mmoX+Y+Z + mmoB + mmoC + mmoD | |
Enzymklassifikation | ||
EC, Kategorie | 1.14.13.25, Monooxygenase | |
Reaktionsart | Addition eines Sauerstoffatoms | |
Substrat | Methan + NAD(P)H + O2 | |
Produkte | Methanol + NAD(P)+ + H2O | |
Vorkommen | ||
Übergeordnetes Taxon | Methanotrophe Bakterien[1] |
Die Methan-Monooxygenase ist ein Multiproteinkomplex mit einer Molekülmasse von 300 kDa. Sie katalysiert die Oxidation des reaktionsträgen Methans zu Methanol in methanotrophen Bakterien, wo es die einzige Kohlenstoff- und Energiequelle darstellt. Modellhaft ausgiebig untersucht wurde das Enzym von Methylococcus capsulatus.
Die Methan-Monooxygenase besteht aus vier Untereinheiten, die A, B, C, D genannt werden, wobei A selbst aus drei weiteren Einheiten α, β und γ aufgebaut ist. Die Gennamen sind mmoX/Y/Z (für A) und mmoB, mmoC, mmoD.
Im aktiven Zentrum der Hydroxylase wird die Methanoxidation mit Hilfe eines dinuklearen Eisenzentrums durchgeführt. Die Eisenatome sind durch sechs Aminosäurereste koordiniert. Damit gehört dieses Enzym in die Klasse der Nicht-Häm-Eisenenzyme.
Literatur
- Murrell JC, Lidstrom ME, Holmes AJ, Costello A (1995). "Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related". FEMS Microbiol. Lett. 132 (3): 203–208. doi:10.1111/j.1574-6968.1995.tb07834.x. PMID 7590173.
- Sayavedra-soto LA, Hommes NG, Arp DJ (2002). "Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea". Arch. Microbiol. 178 (4): 250–255. doi:10.1007/s00203-002-0452-0. PMID 12209257.
- Lieberman RL, Rosenzweig AC (2005). "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane". Nature 434 (7030): 177–182. doi:10.1038/nature03311. PMID 15674245.
- Rosenzweig et al.; Frederick, CA; Lippard, SJ; Nordlund, P (1993). "Crystal structure of bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane". Nature 366 (6455): 537–543. doi:10.1038/366537a0. PMID 8255292.
- Basch, Harold et al. (1999). "Mechanism of the Methane -> Methanol Conversion Reaction Catalyzed by Methane Monooxygenase: A Density Function Study". J. Am. Chem. Soc. 121 (31): 7249–7256. doi:10.1021/ja9906296.
- Nordlund et al.; Sjöberg, BM; Eklund, H (1990). "Three-dimensional structure of the free radical protein of ribonucleotide reductase". Nature 345 (6276): 593–598. doi:10.1038/345593a0. PMID 2190093.
- Nordlund et al.; Eklund, H (1993). "Structure and function of the Escherichia coli ribonucleotide reductase protein R2". J. Mol. Biol. 232 (1): 123–164. doi:10.1006/jmbi.1993.1374. PMID 8331655.
- Liu, K et al. (1995). "Characterization of a Diiron(III) Peroxide Intermediate in the Reaction Cycle of Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath)". J. Am. Chem. Soc 117: 4997. doi:10.1021/ja00122a032.