Functional role of C(alpha)-H...O hydrogen bonds between transmembrane alpha-helices in photosystem I

The crystal structure at 2.5A resolution of the membrane-intrinsic, homotrimeric photosystem I (PSI) isolated from the thermophilic cyanobacterium Synechococcus elongatus shows that each monomer is composed of 12 protein subunits of which nine are embedded in the membrane and feature a total of 34 transmembrane alpha-helices (TMH). Hence, PSI provides an ideal case to study "conventional" and C(alpha)-H...O hydrogen bonds between TMH engaged in intra- and intersubunit interactions. Of the total of 75 C(alpha)-H...O hydrogen bonds between TMHs, 72 are intrasubunit and only three are intersubunit. The two largest subunits PsaA and PsaB are each folded into 11 TMHs showing 29 and 24 intrasubunit C(alpha)-H...O hydrogen bonds, respectively, that are not distributed randomly but many of them flank chlorophyll a (Chl a) co-ordinating amino acids, suggesting stabilisation of these structural segments. As major constituent of the trimerisation domain, subunit PsaL is located next to the 3-fold axis relating the three monomers of PSI. PsaL features a unique number of 19 intrasubunit C(alpha)-H...O hydrogen bonds that connect two of its three TMHs but there are no intersubunit C(alpha)-H...O hydrogen bonds between the three PsaL. Of the three intersubunit C(alpha)-H...O hydrogen bonds, two are formed between PsaA and PsaB and one between PsaB and PsaM. The large number of 75 C(alpha)-H...O hydrogen bonds contrasts the 49 conventional hydrogen bonds, indicating that the former and van der Waals contacts determine association and orientation of TMHs in PSI.