Exploration of Nitrate Reductase Metabolic Pathway in Corynebacterium pseudotuberculosis

Table 3

Residues analyzed regarding the conservation between the narGHI protein sequences of E. coli and C. pseudotuberculosis.

E. coli	C. pseudotuberculosis	Conservation (%)	Function	REF
Residues NarG
His49(H)	His55	100	Mo ion coordination	[42]
Cys53(C)	Cys 59	100	Mo ion coordination	[42]
Cys57(C)	Cys 63	100	Mo ion coordination	[42]
Cys92(C)	Cys 98	100	Mo ion coordination	[42]
Asp222 (D)	Asp 228	100	Mo-bisMGD ligand	[42]
Val 578 (V)	Val 584	100	Left relatively hydrophobic environment to allow binding within the active site, with one face of the side chain carboxylate exposed of Asp222. Optimal interaction with the Mo of the cofactor	[43]
Tyr 220 (Y)	Tyr 226	100	Left relatively hydrophobic environment to allow binding to within the active site, with one face of the side chain carboxylate exposed of Asp222. Allowing optimal interaction with the Mo of the cofactor	[43]
His1092(H)	His 1099	100	Form a hydrogen bond network that links the solvent interface with and could be important for structural integrity and/or proton delivery to the active site	[42]
His1098(H)	His 1105	100	Form a hydrogen bond network that links the solvent interface with and could be important for structural integrity and/or proton delivery to the active site	[42]
His1163(H)	His 1170	100	Form a hydrogen bond network that links the solvent interface with and could be important for structural integrity and/or proton delivery to the active site	[42]
Arg 94(R)	Arg 100	100	Forms a hydrogen bond with the Cys92 ligand of FS0	[43]
Residues NarH
Cys196 (C)	Cys 196	100	Binding of iron atoms of FS4 cluster	[44]
Cys217(C)	Cys 217	100	Binding of iron atoms of FS4 cluster	[44]
Cys223(C)	Cys 223	100	Binding of iron atoms of FS4 cluster	[44]
Cys184(C)	Cys 184	100	Binding of iron atoms of FS3 cluster	[44]
Cys187(C)	Cys 187	100	Binding of iron atoms of FS3 cluster	[44]
Cys192(C)	Cys 192	100	Binding of iron atoms of FS3 cluster	[44]
Cys 227(C)	Cys 227	100	Binding of iron atoms of FS3 cluster	[44]
Cys26(C)	Cys 26	100	Binding of iron atoms of FS2 cluster	[44]
Cys244(C)	Cys 244	100	Binding of iron atoms of FS2 cluster	[44]
Cys247(C)	Cys 247	100	Binding of iron atoms of FS2 cluster	[44]
Cys259(C)	Cys 259	100	Binding of iron atoms of FS2 cluster	[44]
Cys16(C)	Cys 16	100	Binding of iron atoms of FS1 cluster	[44]
Cys19(C)	Cys 19	100	Binding of iron atoms of FS1 cluster	[44]
Cys22(C)	Cys 22	100	Binding of iron atoms of FS1 cluster	[44]
Cys263 (C)	Cys 263	100	Binding of iron atoms of FS1 cluster	[44]
Residues NarI
His66 (H)	His66	100	Iron atoms coordination of heme	[43]
His187 (H)	His190	100	Iron atoms coordination of heme	[43]
His56 (H)	His56	100	Iron atoms coordination of heme	[43]
His205 (H)	His208	100	Iron atoms coordination of heme	[43]
Arg112	Arg113	100	Hydrogen bond network electron transfer between the redox center , FS4, and NarG	[43]
Arg202	Arg205	100	Hydrogen bond network electron transfer between the redox center , FS4, and NarG.	[43]
Ser39	Ser39	100	Hydrogen bond network electron transfer between the redox center , FS4, and NarG.	[43]
Ser40	Ser40	100	Hydrogen bond network electron transfer between the redox center , FS4, and NarG.	[43]
Tyr213(Y)	Tyr216	100	Involved in electrostatic interactions and hydrogen bond, are involved in the formation of NarGHI heterotrimer	[43]
Arg216(R)	Arg219	100	Involved in electrostatic interactions and hydrogen bond, are involved in the formation of NarGHI heterotrimer	[43]
Arg222(R)	Arg225	100	Involved in electrostatic interactions and hydrogen bond, are involved in the formation of NarGHI heterotrimer	[43]
Ser201(S)	Ser204	100	A strong link at Ser201 of NarI allows distinctly shorter distances between the hemes in NarI than the distances observed between the hemes in the cytochrome bc1 complex	[43]

Shown is the position of the residues at E. coli and C. pseudotuberculosis sequences and as well as the function of each residue in the E. colinarGHI structure.