View source for 7mh9


==Crystal structure of R. sphaeroides Photosynthetic Reaction Center variant; Y(M210)3-nitrotyrosine==
<StructureSection load='7mh9' size='340' side='right'caption='[[7mh9]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7mh9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MH9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7mh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mh9 OCA], [https://pdbe.org/7mh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mh9 RCSB], [https://www.ebi.ac.uk/pdbsum/7mh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mh9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RCEH_CERS4 RCEH_CERS4] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Photosynthetic reaction centers (RCs) from Rhodobacter sphaeroides were engineered to vary the electronic properties of a key tyrosine (M210) close to an essential electron transfer component via its replacement with site-specific, genetically encoded noncanonical amino acid tyrosine analogs. High fidelity of noncanonical amino acid incorporation was verified with mass spectrometry and X-ray crystallography and demonstrated that RC variants exhibit no significant structural alterations relative to wild type (WT). Ultrafast transient absorption spectroscopy indicates the excited primary electron donor, P*, decays via a approximately 4-ps and a approximately 20-ps population to produce the charge-separated state P(+)H(A)(-) in all variants. Global analysis indicates that in the approximately 4-ps population, P(+)H(A)(-) forms through a two-step process, P*--&gt; P(+)B(A)(-)--&gt; P(+)H(A)(-), while in the approximately 20-ps population, it forms via a one-step P* --&gt; P(+)H(A)(-) superexchange mechanism. The percentage of the P* population that decays via the superexchange route varies from approximately 25 to approximately 45% among variants, while in WT, this percentage is approximately 15%. Increases in the P* population that decays via superexchange correlate with increases in the free energy of the P(+)B(A)(-) intermediate caused by a given M210 tyrosine analog. This was experimentally estimated through resonance Stark spectroscopy, redox titrations, and near-infrared absorption measurements. As the most energetically perturbative variant, 3-nitrotyrosine at M210 creates an approximately 110-meV increase in the free energy of P(+)B(A)(-) along with a dramatic diminution of the 1,030-nm transient absorption band indicative of P(+)B(A)(-) formation. Collectively, this work indicates the tyrosine at M210 tunes the mechanism of primary electron transfer in the RC.

Photosynthetic reaction center variants made via genetic code expansion show Tyr at M210 tunes the initial electron transfer mechanism.,Weaver JB, Lin CY, Faries KM, Mathews II, Russi S, Holten D, Kirmaier C, Boxer SG Proc Natl Acad Sci U S A. 2021 Dec 21;118(51):e2116439118. doi: , 10.1073/pnas.2116439118. PMID:34907018<ref>PMID:34907018</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7mh9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cereibacter sphaeroides]]
[[Category: Large Structures]]
[[Category: Boxer SG]]
[[Category: Mathews I]]
[[Category: Weaver J]]