Literature DB >> 30726074

Preliminary Assignment of Protonated and Deprotonated Homocitrates in Extracted FeMo-Cofactors by Comparisons with Molybdenum(IV) Lactates and Oxidovanadium Glycolates.

Wan-Ting Jin1, Hongxin Wang2,3, Si-Yuan Wang1, Christie H Dapper4, Xing Li1, William E Newton4, Zhao-Hui Zhou1, Stephen P Cramer2,3.   

Abstract

A similar pair of protonated and deprotonated mononuclear oxidovanadium glycolates [VO(Hglyc)(phen)(H2O)]Cl·2H2O (1) and [VO(glyc)(bpy)(H2O)] (2) and a mixed-(de)protonated oxidovanadium triglycolate (NH4)2[VO(Hglyc)2(glyc)]·H2O (3) were isolated and examined. The ≡C-O(H) (≡C-OH or ≡C-O) groups coordinated to vanadium were spectroscopically and structurally identified. The glycolate in 1 features a bidentate chelation through protonated α-hydroxy and α-carboxy groups, whereas the glycolate in 2 coordinates through deprotonated α-alkoxy and α-carboxy groups. The glycolates in 3 coordinate to vanadium through α-alkoxy or α-hydroxy and α-carboxy groups and thus have both protonated ≡C-OH and deprotonated ≡C-O bonds simultaneously. Structural investigations revealed that the longer protonated V-Oα-hydroxy bonds [2.234(2) Å and 2.244(2) Å] in 1 and 3 are close to those of FeV-cofactor (FeV-co) 2.17 Å1 (FeMo-co 2.17 Å2), while deprotonated V-Oα-alkoxy bonds [2, 1.930(2); 3, 1.927(2) Å] were obviously shorter. This shows a similar elongated trend as the Mo-O distances in the previously reported deprotonated vs protonated molybdenum lactates (Wang, S. Y. et al. Dalton Trans. 2018, 47, 7412-7421) and these vanadium and molybdenum complexes have the same local V/Mo-homocitrate structures as those of FeV/Mo-cos of nitrogenases. The IR spectra of these oxidovanadium and the previously synthesized molybdenum complexes including different substituted ≡C-O(H) model compounds show red-shifts for ≡C-OH vs ≡C-O alternation, which further assign the two IR bands of extracted FeMo-co at 1084 and 1031 cm-1 to ≡C-O and ≡C-OH vibrations, respectively. Although the structural data or IR spectra for some of the previously synthesized Mo/V complexes and extracted FeMo-co were measured earlier, this is the first time that the ≡C-O(H) coordinated peaks are assigned. The overall structural and IR results well suggest the coexistence of homocitrates coordinated with α-alkoxy (deprotonated) and α-hydroxy (protonated) groups in the extracted FeMo-co.

Entities:  

Year:  2019        PMID: 30726074      PMCID: PMC6813765          DOI: 10.1021/acs.inorgchem.8b03108

Source DB:  PubMed          Journal:  Inorg Chem        ISSN: 0020-1669            Impact factor:   5.165


  51 in total

1.  Revisiting the Mössbauer Isomer Shifts of the FeMoco Cluster of Nitrogenase and the Cofactor Charge.

Authors:  Ragnar Bjornsson; Frank Neese; Serena DeBeer
Journal:  Inorg Chem       Date:  2017-01-10       Impact factor: 5.165

2.  Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis.

Authors:  C H Kim; W E Newton; D R Dean
Journal:  Biochemistry       Date:  1995-03-07       Impact factor: 3.162

3.  Spectroscopic investigation of FeMo-cofactor. Coenzyme A as one of the probable components of an active site of nitrogenase.

Authors:  L A Levchenko; O S Roschupkina; A P Sadkov; S A Marakushev; G M Mikhailov; Y G Borod'ko
Journal:  Biochem Biophys Res Commun       Date:  1980-10-16       Impact factor: 3.575

4.  Structure and spectroscopy of a bidentate bis-homocitrate dioxo-molybdenum(VI) complex: insights relevant to the structure and properties of the FeMo-cofactor in nitrogenase.

Authors:  Zhao-Hui Zhou; Hongxin Wang; Ping Yu; Marilyn M Olmstead; Stephen P Cramer
Journal:  J Inorg Biochem       Date:  2012-10-08       Impact factor: 4.155

5.  Comparison of hydroxycarboxylato imidazole molybdenum(iv) complexes and nitrogenase protein structures: indirect evidence for the protonation of homocitrato FeMo-cofactors.

Authors:  Si-Yuan Wang; Wan-Ting Jin; Hong-Bin Chen; Zhao-Hui Zhou
Journal:  Dalton Trans       Date:  2018-06-05       Impact factor: 4.390

6.  Comparative assessment of the composition and charge state of nitrogenase FeMo-cofactor.

Authors:  Travis V Harris; Robert K Szilagyi
Journal:  Inorg Chem       Date:  2011-05-05       Impact factor: 5.165

7.  X-ray emission spectroscopy evidences a central carbon in the nitrogenase iron-molybdenum cofactor.

Authors:  Kyle M Lancaster; Michael Roemelt; Patrick Ettenhuber; Yilin Hu; Markus W Ribbe; Frank Neese; Uwe Bergmann; Serena DeBeer
Journal:  Science       Date:  2011-11-18       Impact factor: 47.728

8.  Evidence for interstitial carbon in nitrogenase FeMo cofactor.

Authors:  Thomas Spatzal; Müge Aksoyoglu; Limei Zhang; Susana L A Andrade; Erik Schleicher; Stefan Weber; Douglas C Rees; Oliver Einsle
Journal:  Science       Date:  2011-11-18       Impact factor: 47.728

9.  Low-temperature magnetic-circular-dichroism spectroscopy of the iron-molybdenum cofactor and the complementary cofactor-less MoFe protein of Klebsiella pneumoniae nitrogenase.

Authors:  A E Robinson; A J Richards; A J Thomson; T R Hawkes; B E Smith
Journal:  Biochem J       Date:  1984-04-15       Impact factor: 3.857

10.  QM/MM Study of the Nitrogenase MoFe Protein Resting State: Broken-Symmetry States, Protonation States, and QM Region Convergence in the FeMoco Active Site.

Authors:  Bardi Benediktsson; Ragnar Bjornsson
Journal:  Inorg Chem       Date:  2017-11-06       Impact factor: 5.165

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  1 in total

1.  Assignment of protonated R-homocitrate in extracted FeMo-cofactor of nitrogenase via vibrational circular dichroism spectroscopies.

Authors:  Lan Deng; Hongxin Wang; Christie H Dapper; William E Newton; Sergey Shilov; Shunlin Wang; Stephen P Cramer; Zhao-Hui Zhou
Journal:  Commun Chem       Date:  2020-10-28
  1 in total

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