Analysis of Some Optical Properties of a Native and Reconstituted Photosystem II Antenna Complex, CP29:  Pigment Binding Sites Can Be Occupied by Chlorophyllaor Chlorophyllband Determine Spectral Forms†

Biochemistry ◽  
1997 ◽  
Vol 36 (42) ◽  
pp. 12984-12993 ◽  
Author(s):  
Elisabetta Giuffra ◽  
Giuseppe Zucchelli ◽  
Dorianna Sandonà ◽  
Roberta Croce ◽  
Daniela Cugini ◽  
...  
2009 ◽  
Vol 284 (12) ◽  
pp. 8103-8113 ◽  
Author(s):  
Matteo Ballottari ◽  
Milena Mozzo ◽  
Roberta Croce ◽  
Tomas Morosinotto ◽  
Roberto Bassi

2003 ◽  
Vol 84 (4) ◽  
pp. 2517-2532 ◽  
Author(s):  
Roberta Croce ◽  
Marc G. Müller ◽  
Stefano Caffarri ◽  
Roberto Bassi ◽  
Alfred R. Holzwarth

Biochemistry ◽  
2020 ◽  
Vol 59 (35) ◽  
pp. 3216-3224 ◽  
Author(s):  
Keisuke Saito ◽  
Manoj Mandal ◽  
Hiroshi Ishikita

1991 ◽  
Vol 46 (7-8) ◽  
pp. 557-562 ◽  
Author(s):  
A. Trebst

Abstract A new contact site between the two reaction center polypeptides D 1 and D 2 of photosystem II close to arg 238 and arg 234 respectively is proposed. The amino acid sequences involved are between the 4 th transmembrane and a connecting parallel helix. The sequence includes a tryp­ sin sensitive site in both polypeptides, the likely cleavage site in the rapid turnover of the D 1 polypeptide and part of the herbicide binding site. The contact site is oriented towards both quinone binding sites Q A and Q B. A folding of the backbone of the amino acid sequences involved is proposed.


1993 ◽  
Vol 48 (3-4) ◽  
pp. 191-198 ◽  
Author(s):  
Simon P. Mackay ◽  
Patrick J. O ’Malley

Abstract The prefered binding orientations for the herbicide DCMU within the QB-binding site of the D 1 protein model from a photosystem II reaction centre have been determined. Calculation of the intermolecular energy between the herbicide and the binding site has been instrumental in obtaining optimum positions reinforced by experimental results from mutation studies and herbicide binding to analogous bacterial reaction centres. We have shown that two binding sites are possible, one involving a hydrogen bond to and the other to the Ser 264 residue. In both cases, which are more important for the stabilization of the interactions.


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