1.14.18.3 ascorbate - 438940 1.14.18.3 duroquinol - 745305 1.14.18.3 duroquinol NADH passes electron to duroquinol 745305 1.14.18.3 additional information - 438940 1.14.18.3 additional information duroquinol as artificial reductant 675831 1.14.18.3 additional information succinate, particulate enzyme functions in vitro with either succinate or NADH as electron donor, soluble enzyme functions only with NADH 438927 1.14.18.3 additional information the pMMO electron donor is generally thought to be ubiquinol generated by a type 2 NADH:quinone oxidoreductase. The addition of cytochrome could facilitate electron transfer without the requirement for NADH 744325 1.14.18.3 NAD+ methane activation by particulate methane monooxygenase is NAD-dependent 746420 1.14.18.3 NAD+ methane activation by particulate methane monooxygenase is NAD-dependent. Docking simulations of NAD+ on the enzyme clearly show preferential binding of the cofactor in the vicinity of the Cu metal centers confirming its functional relationship with particulate methane monooxygenase 746420 1.14.18.3 NADH - 438927, 438944, 438952, 672301, 673739, 674005, 675831, 684112, 686085, 687284, 689789, 702170, 703343, 726954, 727340, 727552, 728079