The FX iron-sulfur cluster serves as the terminal bound electron acceptor in heliobacterial reaction centers.
Phototrophs of the family Heliobacteriaceae contain the simplest known Type I reaction center (RC), consisting of a homodimeric (PshA)(2) core devoid of bound cytochromes and antenna proteins. Unlike plant and cyanobacterial Photosystem I in which the F(A)/F(B) protein, PsaC, is tightly bound to P(700)-F(X) cores, the RCs of Heliobacterium modesticaldum contain two F(A)/F(B) proteins, PshBI and PshBII, which are loosely bound to P(800)-F(X) cores. These two 2[4Fe-4S] ferredoxins have been proposed to function as mobile redox proteins, reducing downstream metabolic partners much in the same manner as does [2Fe-2S] ferredoxin or flavodoxin (Fld) in PS I. Using P(800)-F(X) cores devoid of PshBI and PshBII, we show that iron-sulfur cluster F(X) directly reduces Fld without the involvement of F(A) or F(B) (Fld is used as a proxy for soluble redox proteins even though a gene encoding Fld is not identified in the H. modesticaldum genome). The reduction of Fld is suppressed by the addition of PshBI or PshBII, an effect explained by competition for the electron on F(X). In contrast, P(700)-F(X) cores require the presence of the PsaC, and hence, the F(A)/F(B) clusters for Fld (or ferredoxin) reduction. Thus, in H. modesticaldum, the interpolypeptide F(X) cluster serves as the terminal bound electron acceptor. This finding implies that the homodimeric (PshA)(2) cores should be capable of donating electrons to a wide variety of yet-to-be characterized soluble redox partners.
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Steven P
SP
Romberger
John H
JH
Golbeck
D001426:Bacterial Proteins / Q000378:metabolism; D004579:Electron Transport / Q000502:physiology*; D005288:Ferredoxins / Q000378:metabolism; D006094:Gram-Positive Bacteria / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism; D052817:Phototrophic Processes / Q000502:physiology*
D001426:Bacterial Proteins; D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D045322:Photosynthetic Reaction Center Complex Proteins