8c3f | pdb_00008c3f

Double mutant I(L177)H/F(M197)H structure of Photosynthetic Reaction Center From Cereibacter sphaeroides strain RV

spinqualitylabelsall models 8c3f, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8c3f is a 3 chain structure with sequence from Cereibacter sphaeroides 2.4.1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCL, BPB, CDL, CL, DIO, EDO, FE, GOL, HTO, K, LDA, PO4, SPN, TRS, U10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RCEH_CERSP The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. Publication Abstract from PubMed The photosynthetic reaction center of the purple bacterium Cereibacter sphaeroides with two site-directed mutations Ile-L177-His and M197 Phe-His is of double interest. The substitution I(L177)H results in strong binding of a bacteriochlorophyll molecule with L-subunit. The second mutation F(M197)H introduces a new H-bond between the C2-acetyl carbonyl group of the bacteriochlorophyll P(B) and His-M197, which is known to enhance the stability of the complex. Due to this H-bond, pi -electron system of P finds itself connected to an extensive H-bonding network on the periplasmic surface of the complex. The crystal structure of the double mutant reaction center obtained with 2.6 A resolution allows clarifying consequences of the Ile L177 - His substitution. The value of the P/P(+) midpoint potential in the double mutant RC was found to be ~20 mV less than the sum of potentials measured in the two RCs with single mutations I(L177)H and F(M197)H. The protein environment of the BChls P(A) and B(B) were found to be similar to that in the RC with single substitution I(L177)H, whereas an altered pattern of the H-bonding networks was found in the vicinity of bacteriochlorophyll P(B). The data obtained are consistent with our previous assumption on a correlation between the bulk of the H-bonding network connected with the pi-electron system of the primary electron donor P and the value of its oxidation potential. Properties and Crystal Structure of the Cereibacter sphaeroides Photosynthetic Reaction Center with Double Amino Acid Substitution I(L177)H + F(M197)H.,Fufina TY, Selikhanov GK, Gabdulkhakov AG, Vasilieva LG Membranes (Basel). 2023 Jan 26;13(2):157. doi: 10.3390/membranes13020157. PMID:36837660 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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