scholarly journals Electron transfer protein complexes in the thylakoid membranes of heterocysts from the cyanobacterium Nostoc punctiforme

2009 ◽  
Vol 1787 (4) ◽  
pp. 252-263 ◽  
Author(s):  
Tanai Cardona ◽  
Natalia Battchikova ◽  
Pengpeng Zhang ◽  
Karin Stensjö ◽  
Eva-Mari Aro ◽  
...  
FEBS Journal ◽  
2011 ◽  
Vol 278 (9) ◽  
pp. 1391-1400 ◽  
Author(s):  
Qamar Bashir ◽  
Sandra Scanu ◽  
Marcellus Ubbink

2017 ◽  
Vol 114 (10) ◽  
pp. E1840-E1847 ◽  
Author(s):  
Witold Andrałojć ◽  
Yoshitaka Hiruma ◽  
Wei-Min Liu ◽  
Enrico Ravera ◽  
Masaki Nojiri ◽  
...  

Well-defined, stereospecific states in protein complexes are often in exchange with an ensemble of more dynamic orientations: the encounter states. The structure of the stereospecific complex between cytochrome P450cam and putidaredoxin was solved recently by X-ray diffraction as well as paramagnetic NMR spectroscopy. Other than the stereospecific complex, the NMR data clearly show the presence of additional states in the complex in solution. In these encounter states, populated for a small percentage of the time, putidaredoxin assumes multiple orientations and samples a large part of the surface of cytochrome P450cam. To characterize the nature of the encounter states, an extensive paramagnetic NMR dataset has been analyzed using the Maximum Occurrence of Regions methodology. The analysis reveals the location and maximal spatial extent of the additional states needed to fully explain the NMR data. Under the assumption of sparsity of the size of the conformational ensemble, several minor states can be located quite precisely. The distribution of these minor states correlates with the electrostatic potential map around cytochrome P450cam. Whereas some minor states are on isolated positively charged patches, others are connected to the stereospecific site via positively charged paths. The existence of electrostatically favorable pathways between the stereospecific interaction site and the different minor states or lack thereof suggests a means to discriminate between productive and futile encounter states.


Metallomics ◽  
2014 ◽  
Vol 6 (6) ◽  
pp. 1126-1130 ◽  
Author(s):  
Paul B. Harvilla ◽  
Holly N. Wolcott ◽  
John S. Magyar

The molecular structure of the electron-transfer protein cytochromec552from a cold-adapted, hydrocarbon-degrading marine bacterium is reported (PDB: 4O1W).


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