. Author manuscript; available in PMC: 2010 Sep 8.

Published in final edited form as: J Inorg Biochem. 2007 Apr 19;101(11-12):1630–1641. doi: 10.1016/j.jinorgbio.2007.03.013

Table 5.

Activities and yields of isolated FeMocos

	Activities^a								Yield^b
FeMoco	C₂H₄-formation under C₂H₂/Ar		H₂-formation under Ar		NH₃-formation under N₂		H₂-formation under N₂		FeMoco isolation
	nmol/min/mg protein	%	nmol/min/mg protein	%	nmol/min/mg protein	%	nmol/min/mg protein	%	nmol Mo	%
FeMoco^wild-type	813 ± 145	100	1016 ± 31	100	417 ± 45	100	217 ± 27	100	1430 ± 67	100
FeMoco^αH274A	731 ± 7	90	968 ± 68	95	409 ± 32	98	180 ± 12	83	744 ± 19	52
FeMoco^αH451A	858 ± 44	106	954 ± 52	94	425 ± 23	102	247 ± 27	114	630 ± 31	44
FeMoco^{αH274A/αH451A}	882 ± 20	108	1167 ± 33	115	427 ± 61	102	202 ± 23	93	562 ± 16	39

The activities were determined on the basis of the capabilities of isolated FeMocos to reconstitute Av1^Δ^nifB, a FeMoco-depleted yet P-cluster-replete form of Av1 that can be converted to an active, holo-protein upon FeMoco insertion [18].

The yield of FeMoco was determined by Mo analysis of FeMoco isolated from the same amount (300 mg) of Av1 protein.