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• W2082334879 abstract "Cytochrome f of oxygenic photosynthesis has an unprecedented structure, including the N-terminus being a heme ligand. The adjacent N-terminal heme-shielding domain is enriched in aromatic amino acids. The atomic structures of the chloroplast and cyanobacterial cytochromes f were compared to explain spectral and redox differences between them. The conserved aromatic side chain in the N-terminal heme-shielding peptide at position 4, Phe and Tyr in plants and algae, respectively, and Trp in cyanobacteria, is in contact with the heme. Mutagenesis of cytochrome f from the eukaryotic green alga Chlamydomonas reinhardtii showed that a Phe4 → Trp substitution in the N-terminal domain was unique in causing a red shift of 1 and 2 nm in the cytochrome Soret (γ) and Q (α) visible absorption bands, respectively. The resulting α band peak at 556 nm is characteristic of the cyanobacterial cytochrome. Conversely, a Trp4 → Phe mutation in the expressed cytochrome from the cyanobacterium Phormidium laminosum caused a blue shift to the 554 nm α band peak diagnostic of the chloroplast cytochrome. Residue 4 was found to be the sole determinant of this 60 cm-1 spectral shift, and of approximately one-half of the 70 mV redox potential difference between cytochrome f of P. laminosum and C. reinhardtii (Em7 = 297 and 370 mV, respectively). The proximity of Trp-4 to the heme implies that the spectral and redox potential shifts arise through differential interaction of its σ- or π-electrostatic potential with the heme ring and of the π-potential with the heme Fe orbitals, respectively. The dependence of the visible spectrum and redox potential of cytochrome f on the identity of aromatic residue 4 provides an example of the use of the relatively sharp cytochrome spectrum as a “spectral fingerprint”, and of the novel structural connection between the heme and a single nonliganding residue." @default.
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• W2082334879 date "2000-04-29" @default.
• W2082334879 modified "2023-10-03" @default.
• W2082334879 title "Tryptophan−Heme π-Electrostatic Interactions in Cytochrome <i>f</i> of Oxygenic Photosynthesis" @default.
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• W2082334879 doi "https://doi.org/10.1021/bi9928997" @default.
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