Methylamine interaction with proteins of photosystem II: A comparison with biogenic polyamines

Abstract

Biogenic polyamines are essential for cell growth and differentiation. The interaction of polyamines with protein of photosystem II (PSII) are well investigated, while there has been no report on the effect of monoamines complexation on photosynthetic oxygen evolution. This study was designed to investigate the interaction of methylamine with proteins of PSII, using PSII-enriched submembrane fractions with various concentrations of methylamine. Fourier transformed infrared (FTIR) and fluorescence spectroscopic methods were used in order to determine the methylamine binding mode, the protein conformational changes, and the effect of amine interaction on photosynthetic oxygen evolution. Spectroscopic evidence showed that methylamine interacts with protein (H-bonding) through polypeptide C O, C–N and NH groups with major perturbations of protein secondary structure. Major reduction of α-helix from 50% (free PSII) to 35% with an increase of β-sheet from 10% (free PSII) to 16% was observed in methylamine-PSII complexes. At very low methylamine concentration, no inhibition of oxygen-evolution occurred, while at higher amine content (12 mM), 100% inhibition was observed. Chlorophyll (Chl) fluorescence measurements indicated the inhibition mainly affects the oxygen evolving complex (OEC) of PSII. Comparisons of the effects of methylamine with biogenic polyamine spermine, spermidine and putrescine showed a similar mode of binding with protein (H-bonding) through polypeptide C O, C–N and NH groups. However, major alterations of the protein secondary structure are induced by monoamine and not by polyamines.