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JBIC Journal of Biological Inorganic Chemistry

, Volume 21, Issue 5–6, pp 669–681 | Cite as

Resonance Raman spectroscopic study of the interaction between Co(II)rrinoids and the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri

  • Kiyoung Park
  • Paola E. Mera
  • Jorge C. Escalante-Semerena
  • Thomas C. Brunold
Original Paper
Part of the following topical collections:
  1. E.I. Solomon: Papers in Celebration of His 2016 ACS Alfred Bader Award in Bioorganic or Bioinorganic Chemistry

Abstract

The human-type ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri (LrPduO) catalyzes the adenosylation of Co(II)rrinoids to generate adenosylcobalamin (AdoCbl) or adenosylcobinamide (AdoCbi+). This process requires the formation of “supernucleophilic” Co(I)rrinoid intermediates in the enzyme active site which are properly positioned to abstract the adeonsyl moiety from co-substrate ATP. Previous magnetic circular dichroism (MCD) spectroscopic and X-ray crystallographic analyses revealed that LrPduO achieves the thermodynamically challenging reduction of Co(II)rrinoids by displacing the axial ligand with a non-coordinating phenylalanine residue to produce a four-coordinate species. However, relatively little is currently known about the interaction between the tetradentate equatorial ligand of Co(II)rrinoids (the corrin ring) and the enzyme active site. To address this issue, we have collected resonance Raman (rR) data of Co(II)rrinoids free in solution and bound to the LrPduO active site. The relevant resonance-enhanced vibrational features of the free Co(II)rrinoids are assigned on the basis of rR intensity calculations using density functional theory to establish a suitable framework for interpreting rR spectral changes that occur upon Co(II)rrinoid binding to the LrPduO/ATP complex in terms of structural perturbations of the corrin ring. To complement our rR data, we have also obtained MCD spectra of Co(II)rrinoids bound to LrPduO complexed with the ATP analogue UTP. Collectively, our results provide compelling evidence that in the LrPduO active site, the corrin ring of Co(II)rrinoids is firmly locked in place by several amino acid side chains so as to facilitate the dissociation of the axial ligand.

Keywords

Resonance Raman spectroscopy Density functional theory ATP:corrinoid adenosyltransferase Adenosylcobalamin 

Notes

Acknowledgments

This work was supported in part by the National Science Foundation Grant MCB-0238530 (to T. C. B.), the National Institutes of Health Grant R37-GM40313 (to J. C. E.-S.), the National Research Foundation of Korea NRF-2015R1C1A1A02036917, and the Korea Institute of Science and Technology Information KSC-2015-C2-044 (to K. P.). P. E. M was supported in part by Chemical Biology Interface Training Grant T32-GM008505 (L. L. Kiessling, P. I.) from the National Institute of General Medical Sciences (NIGMS).

Supplementary material

775_2016_1371_MOESM1_ESM.pdf (230 kb)
Supplementary material 1 (PDF 230 kb)

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Copyright information

© SBIC 2016

Authors and Affiliations

  1. 1.Department of ChemistryKorea Advanced Institute of Science and TechnologyDaejeonRepublic of Korea
  2. 2.Department of Chemistry and BiochemistryNew Mexico State UniversityLas CrucesUSA
  3. 3.Department of MicrobiologyUniversity of GeorgiaAthensUSA
  4. 4.Department of ChemistryUniversity of Wisconsin-MadisonMadisonUSA

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