1.6.2.2	FAD	-	392811, 394194, 394222, 394225, 657648, 657949, 658252, 658832, 659107, 659255, 659784, 685672, 696154, 696575, 699061, 711543, 712469, 712873, 713204, 741542, 741995, 742304, 742312, 742321, 742875, 743151, 743832	
1.6.2.2	FAD	1 mol FAD per mol enzyme	394203, 394218	
1.6.2.2	FAD	1 mol FAD per mol of recombinant enzyme	394199	
1.6.2.2	FAD	calculated results suggest that the electron and/or hydride ion transfer reaction from NADH to FAD can be accelerated in the presence of heme(Fe3+)	688620	
1.6.2.2	FAD	cytochrome b5 reductase is composed of one FAD and one NADH binding domain linked by a hinge region	685857	
1.6.2.2	FAD	flavoprotein, the FAD domain has a large cleft in which the FAD prosthetic group is located. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains	724801	
1.6.2.2	FAD	non-covalentely bound prosthetic group	657675	
1.6.2.2	FAD	non-covalently bound in a large cleft between the two major domains	657460	
1.6.2.2	FAD	redox state of FAD during the b5R catalytic cycle and crystal structures comparion of the fully reduced form and the oxidized form, overview	725721	
1.6.2.2	FAD	the FAD cofactor is located in the cleft between the N-terminal FAD-binding domain and the C-terminal NADH-binding domain. The cofactor is located in the cleft between the two domains and interacts primarily with the FAD-binding domain	764860	
1.6.2.2	FAD	the FAD group of cytochrome b5 reductase increases its solvent exposition upon complex formation with cytochrome b5 promoting an efficient electron transfer between the proteins	764211	
1.6.2.2	FAD	tightly bound prosthetic group	657966	
1.6.2.2	heme	-	742308	
1.6.2.2	NAD+	-	741995, 743151	
1.6.2.2	NAD+	NAD+ and NADP+ bind with the nicotinamide ring in the active site	763842	
1.6.2.2	NADH	-	392811, 394194, 394195, 394196, 394197, 394198, 394199, 394200, 394201, 394202, 394203, 394204, 394205, 394206, 394207, 394208, 394209, 394210, 394211, 394212, 394213, 394214, 394215, 394216, 394217, 394218, 394219, 394221, 394222, 394223, 394224, 394225, 394226, 394227, 394228, 394229, 394230, 394231, 394232, 394233, 394234, 394235, 394236, 657460, 657648, 657675, 657966, 658252, 658832, 659107, 659255, 659784, 671983, 672018, 672826, 699061, 711543, 712469, 712873, 713187, 713204, 724717, 725721, 726166, 726519, 726541, 743313	
1.6.2.2	NADH	dependent on	725046, 725047	
1.6.2.2	NADH	marked preference for NADH versus NADPH	671607	
1.6.2.2	NADH	NADH is 5-10 times more active than NADPH in supporting redox cycling	765854	
1.6.2.2	NADH	native enzyme shows 3700fold preference for NADH over NADPH	657949	
1.6.2.2	NADH	preferred electron donor for CyB5R, a D239T mutation will change this preference to one for NADPH. The NADH domain provides a suitable position for the NADH coenzyme. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains	724801	
1.6.2.2	NADH	strict specificity for NADH	676661	
1.6.2.2	NADP+	NAD+ and NADP+ bind with the nicotinamide ring in the active site	763842	
1.6.2.2	NADPH	-	394249, 394252, 671983, 672826	
1.6.2.2	NADPH	1/300 of NADH linked activity	394230	
1.6.2.2	NADPH	7-9% of NADH activity	394210	
1.6.2.2	NADPH	marked preference for NADH versus NADPH	671607	
1.6.2.2	NADPH	NADH is 5-10 times more active than NADPH in supporting redox cycling	765854	
1.6.2.2	NADPH	preferred cofactor for some engineered enzymes	657949