Characterization of the secondary structure and thermostability of the extrinsic 16 kilodalton protein of spinach photosystem II by Fourier transform infrared spectroscopy

Abstract The secondary structure and thermostability of the extrinsic 16 kDa protein of the spinach photosystem II (OEC16) were characterized in solution between 25 and 75°C using Fourier transform infrared (FTIR) spectroscopy. Quantitative analyses of the amide I band (1700–1600 cm−1) showed that the OEC16 subunit contains 34% α-helix, 28% β-sheet, 6% turn, and 32% disorder structures at 25°C. This structural feature differs significantly from that of OEC23 as we had reported previously (H. Zhang, Y. Ishikawa, Y. Yamamoto, R. Carpentier, FEBS Letters 426 (1998) 347–351), although both the OEC subunits are involved in regulating Ca2+ and Cl− requirements. In addition, it was observed that the structure of OEC16 is stable at

[1]  R. Carpentier,et al.  A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of photosystem II by FTIR spectroscopy , 1995, FEBS letters.

[2]  J. Barber,et al.  Structure and thermal stability of photosystem II reaction centers studied by infrared spectroscopy. , 1997, Biochemistry.

[3]  N. Murata,et al.  Partial degradation of the 18-kDa protein of the photosynthetic oxygen-evolving complex: A study of a binding site , 1986 .

[4]  F. Goñi,et al.  Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy. , 1994, Biochemistry.

[5]  H. Hayashi,et al.  Effects of glycinebetaine and unsaturation of membrane lipids on heat stability of photosynthetic electron-transport and phosphorylation reactions in Synechocystis PCC6803 , 1993 .

[6]  J. Messinger,et al.  On the functional significance of substrate accessibility in the photosynthetic water oxidation mechanism , 1996 .

[7]  N. Murata,et al.  Role of the 33‐kDa polypeptide in preserving Mn in the photosynthetic oxygen‐evolution system and its replacement by chloride ions , 1984 .

[8]  C. Jansson,et al.  Reconstitution of photosynthetic water splitting in inside-out thylakoid vesicles and identification of a participating polypeptide , 1982 .

[9]  J. Nugent.  Oxygenic photosynthesis. Electron transfer in photosystem I and photosystem II. , 1996, European journal of biochemistry.

[10]  R. Debus,et al.  The 23 and 17 kDa extrinsic proteins of photosystem II modulate the magnetic properties of the S1-state manganese cluster. , 1998, Biochemistry.

[11]  W. Williams,et al.  Stabilisation of PS-II-mediated electron transport in oxygen-evolving PS II core preparations by the addition of compatible co-solutes. , 1992, Biochimica et biophysica acta.

[12]  H. Hayashi,et al.  Glycinebetaine stabilizes the association of extrinsic proteins with the photosynthetic oxygen‐evolving complex , 1992, FEBS letters.

[13]  H. Hayashi,et al.  Thermal Protection of the Oxygen-Evolving Machinery by PsbU, an Extrinsic Protein of Photosystem II, in Synechococcus species PCC 7002 , 1997, Plant physiology.

[14]  G. Papageorgiou,et al.  Protection of the oxygen-evolving photosystem II complex by glycinebetaine , 1991 .

[15]  A. Seidler.  The extrinsic polypeptides of Photosystem II. , 1996, Biochimica et biophysica acta.

[16]  H. Mantsch,et al.  New insight into protein secondary structure from resolution-enhanced infrared spectra. , 1988, Biochimica et biophysica acta.

[17]  H. Susi,et al.  Examination of the secondary structure of proteins by deconvolved FTIR spectra , 1986, Biopolymers.

[18]  R. Carpentier,et al.  Secondary structure and thermal stability of the extrinsic 23 kDa protein of photosystem II studied by Fourier transform infrared spectroscopy , 1998, FEBS letters.

[19]  R. Debus.  The manganese and calcium ions of photosynthetic oxygen evolution. , 1992, Biochimica et biophysica acta.

[20]  S. Katoh,et al.  Ascorbate-supported NADP photoreduction by heated Euglena chloroplasts. , 1967, Archives of biochemistry and biophysics.

[21]  P. Haris,et al.  Fourier transform infrared spectroscopic studies of calcium-binding proteins , 1991 .

[22]  H. Hayashi,et al.  Photosynthetic Oxygen Evolution Is Stabilized by Cytochrome c550 against Heat Inactivation in Synechococcus sp. PCC 7002 , 1994, Plant physiology.

[23]  J. Berry,et al.  Photosynthetic Response and Adaptation to Temperature in Higher Plants , 1980 .

[24]  H. Mantsch,et al.  Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy. , 1990, Biochemistry.

[25]  Y. Toyoshima,et al.  The role of lipids and 17‐kDa protein in enhancing the recovery of O2 evolution in cholate‐treated thylakoid membranes , 1984 .

[26]  F. Goñi,et al.  Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. , 1993, Progress in biophysics and molecular biology.