Structure-function relationships in the 47-kDa antenna protein and its complex with the photosystem II reaction center core: insights from picosecond fluorescence decay kinetics and resonance Raman spectroscopy

Biochemistry ◽  
1994 ◽  
Vol 33 (6) ◽  
pp. 1455-1466 ◽  
Author(s):  
Julio C. de Paula ◽  
Ann Liefshitz ◽  
Sarina Hinsley ◽  
Wei Lin ◽  
Vikas Chopra ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Photosystem Ii ◽  
Structure Function ◽  
Reaction Center ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Fluorescence Decay ◽  
Decay Kinetics ◽  
Fluorescence Decay Kinetics

scholarly journals Evidence that D1 Processing Is Required for Manganese Binding and Extrinsic Protein Assembly into Photosystem II

2004 ◽  
Vol 279 (44) ◽  
pp. 45417-45422 ◽  
Author(s):  
Johnna L. Roose ◽  
Himadri B. Pakrasi
Keyword(s):  
Photosystem Ii ◽  
Mutant Cell ◽  
Protein A ◽  
D1 Protein ◽  
Fluorescence Decay ◽  
Normal Function ◽  
Temporal Position ◽  
Decay Kinetics ◽  
Fluorescence Decay Kinetics ◽  
Extrinsic Proteins

Photosystem II (PSII) is a large membrane protein complex that catalyzes oxidation of water to molecular oxygen. During its normal function, PSII is damaged and frequently turned over. The maturation of the D1 protein, a key component in PSII, is a critical step in PSII biogenesis. The precursor form of D1 (pD1) contains a C-terminal extension, which is removed by the protease CtpA to yield PSII complexes with oxygen evolution activity. To determine the temporal position of D1 processing in the PSII assembly pathway, PSII complexes containing only pD1 were isolated from a CtpA-deficient strain of the cyanobacteriumSynechocystis6803. Although membranes from the mutant cell had nearly 50% manganese, no manganese was detected in isolated ΔctpAHT3 PSII, indicating a severely decreased manganese affinity. However, chlorophyll fluorescence decay kinetics after a single saturating flash suggested that the donor YZwas accessible to exogenous Mn2+ions. Furthermore, the extrinsic proteins PsbO, PsbU, and PsbV were not present in PSII isolated from this mutant. However, PsbO and PsbV were present in mutant membranes, but the amount of PsbV protein was consistently less in the mutant membranes compared with the control membranes. We conclude that D1 processing precedes manganese binding and assembly of the extrinsic proteins into PSII. Interestingly, the Psb27 protein was found to be more abundant in ΔctpAHT3 PSII than in HT3 PSII, suggesting a possible role of Psb27 as an assembly factor during PSII biogenesis.

scholarly journals Probing Protein Secondary Structure Influence on Active Centers with Hetero Two-Dimensional Correlation (Resonance) Raman Spectroscopy: A Demonstration on Cytochrome C

2021 ◽  
pp. 000370282110289
Author(s):  
Julian Hniopek ◽  
Thomas Bocklitz ◽  
Michael Schmitt ◽  
Jürgen Popp
Keyword(s):  
Raman Spectroscopy ◽  
Structure Function ◽  
Active Center ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Two Dimensional ◽  
Active Centers ◽  
Structure Function Relationship ◽  
Function Relationship ◽  
Relationship Of

The functionality of active centers in proteins is governed by the secondary and higher structure of proteins which often lead to structures in the active center that are different from the structures found in protein-free models of the active center. To elucidate this structure–function relationship, it is therefore necessary to investigate both the protein structure and the local structure of the active center. In this work, we investigate the application of hetero (resonance) Raman two-dimensional correlation spectroscopy (2D-COS) to this problem. By employing a combination of near-infrared-Fourier transform-Raman- and vis-resonance Raman spectroscopy, we could show that this combination of techniques is able to directly probe the structure–function relationship of proteins. We were able to correlate the transition of the heme center in cytochrome c from low to high spin with changes in the secondary structure with the above mentioned two spectroscopic in situ techniques and without sample preparation. Thereby, we were able to reveal that the combination of a spectroscopic method to selectively observe the active center with a technique that monitors the whole system offers a promising toolkit to investigate the structure–function relationship of proteins with photoactive centers in general.

Resonance Raman spectroscopy of carotenoids in Photosystem II core complexes

2005 ◽  
Vol 83 (1) ◽  
pp. 45-52 ◽  
Author(s):  
Cara A. Tracewell ◽  
Agnes Cua ◽  
David F. Bocian ◽  
Gary W. Brudvig
Keyword(s):  
Raman Spectroscopy ◽  
Photosystem Ii ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman
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