1.14.18.3 Co2+ the enzyme contains three Co2+ ions per enzyme molecule 672301 1.14.18.3 copper an anomalous site modeled as a dinuclear copper cluster. The mononuclear copper site is absent (one His is not conserved), and the zinc replaced by a copper ion 703343 1.14.18.3 copper contains 2.3 copper ions per 100 kDa protomer 727340 1.14.18.3 copper contains 20.8 copper ions per 100 kDa protomer 727340 1.14.18.3 copper contains 4.8 copper ions per 100 kDa protomer 727340 1.14.18.3 copper contains both mononuclear copper and a copper-containing cluster. Each 200000 Da pMMO complex contains 4.8 copper ions. The purified particulate methane monooxygenase is a mixture of Cu(I) and Cu(II) oxidation states 660351 1.14.18.3 copper regulates the metabolic switch between the methane monooxygenase and the methane monooxygenase-NADH:quinone oxidoreductase complex, also regulates the level of expression of the pMMO and the development of internal membranes 659033 1.14.18.3 copper required, activates 671965 1.14.18.3 copper the enzyme contains 13 copper ions 728079 1.14.18.3 copper the enzyme contains a dicopper center 727681 1.14.18.3 copper the enzyme contains about 2.3 copper ions per 100 kDa protomer the enzyme contains a mixture of Cu+ and Cu2+ 726954 1.14.18.3 copper the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron 745389 1.14.18.3 copper the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase 746420 1.14.18.3 copper the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme. The copper ion interacts with three or four nitrogenic ligands, EPR-active copper 657810 1.14.18.3 Cu+ pMMO, requirement for, contains 12-15 Cu+ ions per molecule of enzyme 438952 1.14.18.3 Cu+ the C-terminal domain of PmoB in pMMO is a reservoir for Cu(I) with properties similar to those of the E-cluster copper ions in the intact holoenzyme 685113 1.14.18.3 Cu2+ 14.5 atoms per molecule of enzyme pMMO, type II copper centre 438944 1.14.18.3 Cu2+ a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity 745721 1.14.18.3 Cu2+ absolutely required, quantum refinement does not support dinuclear copper sites in crystal structures of particulate methane monooxygenase, copper content and binding structure analysis, crystal structures analysis from PDB IDs 3RGB and 3RFR, and modeling, QM-refined structures, detailed overview. Putative mechanism for the reaction of the mononuclear site with methane 744037 1.14.18.3 Cu2+ an integral membrane metalloenzyme, the enzyme has a dicopper active site, structures of the dicopper site of enzyme pMMO, overview. Possible peroxo state of the dicopper site of pMMO from combined quantum mechanics and molecular mechanics calculations. The pMMO active site is considered to contain two Cu ions with a Cu-Cu distance of about 2.58 A within the pmoB subunit. One copper is coordinated by two histidine imidazoles, and another is chelated by a histidine imidazole and primary amine of an N-terminal histidine. The QM region contains the two Cu ions, His33, His137, His139, Tyr374, and Glu35 for the resting state, and, in addition, two oxygen atoms for the peroxo state 745067 1.14.18.3 Cu2+ contains a mononuclear and a dinculear Cu2+ center in the soluble domain of the 47 kDa subunit 684112 1.14.18.3 Cu2+ copper genetically regulates the enzyme activity of the soluble and membrane-bound form 438927 1.14.18.3 Cu2+ Cu2+ is involved in the active site of pMMOH 690034 1.14.18.3 Cu2+ increases enzyme expression and activity of the enzyme in recombinant Rhodococcus erythropolis strain LSSE8-1 673739 1.14.18.3 Cu2+ multi-copper enzyme with 14.1 copper atoms per protein, highest specific activity is observed wit 0.04 mM Cu2+ in the growth medium 716108 1.14.18.3 Cu2+ multicopper enzyme, contains 3 Cu2+ ions per trimer, contains 13.6 copper atoms per protein complex 684114 1.14.18.3 Cu2+ pMH contains 2-4 atoms of copper per a minimum molecular weight of 99 kDa 702501 1.14.18.3 Cu2+ pMMO contains a dicopper center and a mononuclear copper center, As-isolated enzyme conatins 10.2 Cu2+ equivalents per 100 kDa pMMO 716109 1.14.18.3 Cu2+ pmMO contains copper ions (150 nmol per mg protein in membrane fractions) that are required for its enzymatic activity. Some increase in pMMO activity is observed by adding CuSO4 716110 1.14.18.3 Cu2+ pMMO contains tightly bound copper, EDTA has no effect 438951 1.14.18.3 Cu2+ purified pMMO contains 2-3 coppers 705192 1.14.18.3 Cu2+ required 745305 1.14.18.3 Cu2+ required for activity 701759 1.14.18.3 Cu2+ required for activity, each of pmoA, pmoB, and pmoC houses a dicopper center 746420 1.14.18.3 Cu2+ required for activity, enzyme pMMO has a copper active site. dicopper site occupied with a two copper ions or b one copper ion from Methylocystis speciesstrain M, structure comparisons, modeling 745389 1.14.18.3 Cu2+ required for activity, enzyme pMMO has a copper active site. Subdomain with a Cu-Cu distance of about 2.5 A, ligated by the N-terminal amino group and side chain of His33 (Cu1) as well as His137 and His139 (Cu2), and a zinc ion in PmoC about 20 A away from the PmoB dicopper site and attributed to the crystallization solution 745389 1.14.18.3 Cu2+ required, preferred metal ion 745305 1.14.18.3 Cu2+ stimulation by methanobactin-Cu2+ complex, no activation in absence of methanobactin 675831 1.14.18.3 Cu2+ the active enzyme contains approximately 15 copper atoms per mol 438942 1.14.18.3 Cu2+ the active enzyme contains approximately 15 copper atoms per mol enzyme 438942 1.14.18.3 Cu2+ the dicopper site is located at the N-terminus of the pmoB subunit, and conserved residues His33, His137, and His139 coordinate the copper ions. Copper center modeling: the first site is modeled as a single copper ion coordinated by residues His48 and His72 and is not present in other pMMOs. The second site, located near the membrane interface, is coordinated by residues His33, His137, and His139 and is highly conserved among pMMOs and related enzymes. The EPR measurements indicate that the dicopper site in pMMO contains one Cu(I) ion and one Cu(II) ion, proposed as a valence-localized mixed-valence Cu(I)Cu(II) pair, and that the monocopper site is present as Cu(I). The 1H ENDOR measurements show that the Cu(II) is not coordinated by a HxO ligand, so the two ions of the Cu(I)Cu(II) pair cannot be bridged by a hydroxo group in the as-isolated samples. The measurements do not rule out an oxo bridge 745154 1.14.18.3 Cu2+ the enzyme complex contains multiple copper ions, 12-15 copper ions per protein monomer 744405 1.14.18.3 Cu2+ the enzyme contains a mononuclear copper center and a dinuclear copper center, Cu-Cu interaction occurs in all redox forms of the enzyme, usage of mixed-valent dinuclear Cu model compounds, [tris{(N'-tert-butylureaylato)-N-ethyl}aminatocopper(II)]2BF4, and [N-tert-butylurealylato-{2-(dimethylamino)ethyl}aminatocopper(II)]2BF4, which are blue, and purple samples of [Cu2(m-xylylenediaminebis(Kemp’s triacid imide))(my-OTf)(THF)2], and [Cu2(m-xylylenediaminebis(Kemp’s triacid imide))(my-O2CCF3)(THF)2], EXAFS and Fourier transformation analysis, detailed interaction analysis, overview 674005 1.14.18.3 Cu2+ the enzyme is stimulated by exogenous copper (348% activity at 0.4 mM) 713934 1.14.18.3 Cu2+ the enzyme possesses a dicopper center 712040 1.14.18.3 Cu2+ two metal sites: a dicopper centre coordinated by histidine residues in subunit-B and a variable-metal site coordinated by carboxylate and histidine residues from subunit-C. A metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity 745721 1.14.18.3 Fe pMMOH bears a binuclear iron valence site [Fe(III)-Fe(IV)] 690034 1.14.18.3 Fe2+ As-isolated enzyme conatins 1.31 Fe2+ equivalents per 100 kDa pMMO 716109 1.14.18.3 Fe2+ pmMO contains 450 nmol Fe2+ per mg protein in membrane fractions 716110 1.14.18.3 Fe2+ the active enzyme contains 2 iron atoms per mol 438942 1.14.18.3 Fe2+ the active enzyme contains 2 iron atoms per mol enzyme 438942 1.14.18.3 Fe2+ the enzyme contains about 0.6 Fe2+ ions per 100 kDa protomer 726954 1.14.18.3 Fe2+ the enzyme contains one Fe2+ ion per enzyme molecule 672301 1.14.18.3 Fe3+ contains a diiron(III) center 687284 1.14.18.3 Fe3+ presence of an octahedral environment that may well be exchange-coupled to another paramagnetic species 657810 1.14.18.3 Iron 2.5 atoms per enzyme molecule of pMMO 438944 1.14.18.3 Iron each 200000 Da pMMO complex contains 1.5 iron ions 660351 1.14.18.3 Iron pMH contains 1 or 2 atoms of nonheme iron 702501 1.14.18.3 Iron the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme, contains EPR-silent iron 657810 1.14.18.3 Mn2+ pMMO, low content 438944 1.14.18.3 Mo2+ pMMO, low content 438944 1.14.18.3 additional information analysis of the oxidation states and coordination environments of the pMMO metal centers, overview 674005 1.14.18.3 additional information copper-induced iron-uptake 438944 1.14.18.3 additional information increase of activity is not observed by adding FeSO4 716110 1.14.18.3 additional information metal content of Methylococcus capsulatus (Bath) crude membranes before (as-isolated) and after (apo) cyanide treatment, and of apo-membranes after zinc and zinc/copper loading, overview. When zinc is loaded first, copper can replace one zinc site, which is likely the more accessible pmoC site. The activity of the zinc- and copper-loaded membrane-bound pMMO is 11-18% of the copper-reconstituted membrane-bound pMMO activity. This activity is lower than the 40-60% observed for copper- and zinc-loaded pMMO, even though the metal stoichiometries are similar, which is consistent with zinc occupying the active site when loaded first 745305 1.14.18.3 additional information purified pMMO contains no iron per pMMO protomer 705192 1.14.18.3 additional information purified pMMO does not contain zinc in the trans-membrane domain 703343 1.14.18.3 additional information the final model for the zinc-soaked structure included pmoB residues 29-418, pmoA residues 9-252, and pmoC residues 16-210 and 224-256, three polyalanine helices consisting of up to 25 residues, five zinc ions, three copper ions, and one cacodylate molecule 745305 1.14.18.3 additional information the pMMO active site might possess a di-iron center located at the transmembrane zinc/copper site 746420 1.14.18.3 additional information Zn2+ is not associated with purified pMMO 684112 1.14.18.3 Zinc contains zinc 727340 1.14.18.3 Zn2+ binds in the copper active site 745389 1.14.18.3 Zn2+ can replace Cu2+, enzyme-bound, structure analysis, overview. Zinc binding at the pmoC site in the zinc-soaked structure stabilizes pmoC residues 200-210 745305 1.14.18.3 Zn2+ contains one Zn2+ ion in the transmembrane domain 684114 1.14.18.3 Zn2+ enzyme bound, structure analysis, overview 745305 1.14.18.3 Zn2+ enzyme-bound 746420 1.14.18.3 Zn2+ increases enzyme expression and activity of the enzyme in recombinant Rhodococcus erythropolis strain LSSE8-1 673739 1.14.18.3 Zn2+ one Zn2+ ion is bound per enzyme molecule 744037 1.14.18.3 Zn2+ pMMO 438944 1.14.18.3 Zn2+ pmMO contains 1.5 nmol Zn2+ per mg protein in membrane fractions 716110 1.14.18.3 Zn2+ the enzyme contains a nonphysiological mononuclear zinc center 674005