Dataset Information

Affinity and activity of non-native quinones at the Q(B) site of bacterial photosynthetic reaction centers.

ABSTRACT: Purple, photosynthetic reaction centers from Rhodobacter sphaeroides bacteria use ubiquinone (UQ10) as both primary (Q(A)) and secondary (Q(B)) electron acceptors. Many quinones reconstitute Q(A) function, while a few will act as Q(B). Nine quinones were tested for their ability to bind and reconstitute Q(A) and Q(B) functions. Only ubiquinone (UQ) reconstitutes both functions in the same protein. The affinities of the non-native quinones for the Q(B) site were determined by a competitive inhibition assay. The affinities of benzoquinones, naphthoquinone (NQ), and 2-methyl-NQ for the Q(B) site are 7 ± 3 times weaker than that at Q(A) site. However, di-ortho-substituted NQs and anthraquinone bind tightly to the Q(A) site (K d ? 200 nM), and ?1,000 times more weakly to the Q(B) site, perhaps setting a limit on the size of the site. With a low-potential electron donor, 2-methyl, 3-dimethylamino-1,4-NQ, (Me-diMeAm-NQ) at Q(A), Q(B) reduction is 260 meV, more favorable than with UQ as Q(A). Electron transfer from Me-diMeAm-NQ at the Q(A) site to NQ at the Q(B) site can be detected. In the Q(B) site, the NQ semiquinone is estimated to be ?60-100 meV higher in energy than the UQ semiquinone, while in the Q(A) site, the semiquinone energy level is similar or lower with NQ than with UQ. Thus, the NQ semiquinone is more stable in the Q(A) than in the Q(B) site. In contrast, the native UQ semiquinone is ?60 meV lower in energy in the Q(B) than in the Q(A) site, stabilizing forward electron transfer from Q(A) to Q(B).

SUBMITTER: Zhang X

PROVIDER: S-EPMC4442677 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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Affinity and activity of non-native quinones at the Q(B) site of bacterial photosynthetic reaction centers.

Zhang Xinyu X Gunner M R MR

Photosynthesis research 20130529 1-2

Purple, photosynthetic reaction centers from Rhodobacter sphaeroides bacteria use ubiquinone (UQ10) as both primary (Q(A)) and secondary (Q(B)) electron acceptors. Many quinones reconstitute Q(A) function, while a few will act as Q(B). Nine quinones were tested for their ability to bind and reconstitute Q(A) and Q(B) functions. Only ubiquinone (UQ) reconstitutes both functions in the same protein. The affinities of the non-native quinones for the Q(B) site were determined by a competitive inhibi ...[more]

PMID: 23715773

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Project description:Previously we have shown that ONIOM type (QM/MM) calculations can be used to simulate isotope edited FTIR difference spectra for neutral ubiquinone in the QA binding site in Rhodobacter sphaeroides photosynthetic reaction centers. Here we considerably extend upon this previous work by calculating isotope edited FTIR difference spectra for reaction centers with a variety of unlabeled and (18)O labeled foreign quinones incorporated into the QA binding site. Isotope edited spectra were calculated for reaction centers with 2,3-dimethoxy-5,6-dimethyl-1,4-benzoquinone (MQ0), 2,3,5,6-tetramethyl-1, 4-benzoquinone (duroquinone, DQ), and 2,3-dimethyl-l,4-naphthoquinone (DMNQ) incorporated, and compared to corresponding experimental spectra. The calculated and experimental spectra agree well, further demonstrating the utility and applicability of our ONIOM approach for calculating the vibrational properties of pigments in protein binding sites. The normal modes that contribute to the bands in the calculated spectra, their composition, frequency, and intensity, and how these quantities are modified upon (18)O labeling, are presented. This computed information leads to a new and more detailed understanding/interpretation of the experimental FTIR difference spectra. Hydrogen bonding to the carbonyl groups of the incorporated quinones is shown to be relatively weak. It is also shown that there is some asymmetry in hydrogen bonding, accounting for 10-13 cm(-1) separation in the frequencies of the carbonyl vibrational modes of the incorporated quinones. The extent of asymmetry in H-bonding could only be established by considering the spectra for various types of quinones incorporated into the QA binding site. The quinones listed above are "tail-less." Spectra were also calculated for reaction centers with corresponding "tail" containing quinones incorporated, and it is found that replacement of the quinone methyl group by a phytyl or prenyl chain does not alter ONIOM calculated spectra.

Project description:Reaction centers (RCs) are integral membrane proteins that undergo a series of electron transfer reactions during the process of photosynthesis. In the Q(A) site of RCs from Rhodobacter sphaeroides, ubiquinone-10 is reduced, by a single electron transfer, to its semiquinone. The neutral quinone and anionic semiquinone have similar affinities, which is required for correct in situ reaction thermodynamics. A previous study showed that despite similar affinities, anionic quinones associate and dissociate from the Q(A) site at rates ≈10(4) times slower than neutral quinones indicating that anionic quinones encounter larger binding barriers (Madeo, J.; Gunner, M. R. Modeling binding kinetics at the Q(A) site in bacterial reaction centers. Biochemistry 2005, 44, 10994-11004). The present study investigates these barriers computationally, using steered molecular dynamics (SMD) to model the unbinding of neutral ground state ubiquinone (UQ) and its reduced anionic semiquinone (SQ(-)) from the Q(A) site. In agreement with experiment, the SMD unbinding barrier for SQ(-) is larger than for UQ. Multi Conformational Continuum Electrostatics (MCCE), used here to calculate the binding energy, shows that SQ(-) and UQ have comparable affinities. In the Q(A) site, there are stronger binding interactions for SQ(-) compared to UQ, especially electrostatic attraction to a bound non-heme Fe(2+). These interactions compensate for the higher SQ(-) desolvation penalty, allowing both redox states to have similar affinities. These additional interactions also increase the dissociation barrier for SQ(-) relative to UQ. Thus, the slower SQ(-) dissociation rate is a direct physical consequence of the additional binding interactions required to achieve a Q(A) site affinity similar to that of UQ. By a similar mechanism, the slower association rate is caused by stronger interactions between SQ(-) and the polar solvent. Thus, stronger interactions for both the unbound and bound states of charged and highly polar ligands can slow their binding kinetics without a conformational gate. Implications of this for other systems are discussed.

Dataset Information

Affinity and activity of non-native quinones at the Q(B) site of bacterial photosynthetic reaction centers.

Publications

Affinity and activity of non-native quinones at the Q(B) site of bacterial photosynthetic reaction centers.

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