Spectroscopic studies on peptides and proteins with cysteine-containing heme regulatory motifs (HRM)

Schubert, E.; Florin, Nicole; Duthie, F.G.; Brewitz, Hans Henning; Kühl, Toni; Imhof, Diana; Hagelueken, Gregor; Schiemann, Olav

doi:10.1016/j.jinorgbio.2015.05.008

Cited by 25 publications

(39 citation statements)

References 28 publications

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“…Such ac omplex clearly meets the criteria for transient heme binding to HRMs in proteins. Electron paramagnetic resonance (EPR) spectroscopic investigations indicated ah igh spin state of the Fe III heme complex with peptide 8; [18] this supports the observation of pentacoordination obtained by resonance Raman spectroscopy in this study.I nterestingly,p eptides 15 and 27 also revealed ap entacoordinated state in resonance Raman spectroscopy.E ach of the peptides possesses at least one Tyr residue, but no His residue in its sequence. This indicates an obvious difference between His and Tyrr esidues with regard to provision of additional coordination sites.…”

Section: Investigation Of Complex Geometry By Resonance Raman Spectrosupporting

confidence: 90%

“…In our study,t he NMR spectra for 11, 18, 21,a nd 30 each showed only one distinct signal set upon binding of Ga III PPIX, indicating in most of these cases (18,21,30)apentacoordinated-although for one sequence (peptide 11)ahexacoordinated-bound state. In contrast, the NMR spectra for 8 exhibited multiple signal sets indicating as ymmetry break upon Ga III PPIX association,w hichc ouldo nly be explainedi nt erms of an asymmetrichexacoordination.…”

Section: Nmr Studies Of Selected Heme-binding Peptidesmentioning

confidence: 52%

“…The occurrence of hexacoordinated heme iron ions in mixtures containing peptides 10 , 11 , 30 , and 32 may be attributed to the presence of an additional coordinating amino acid such as His or Tyr (peptide classes II and IV). The observations of mixtures of penta‐ and hexacoordinated complexes for 11 and 30 are consistent with EPR data from an earlier study …”

Section: Resultsmentioning

confidence: 91%

“…This set is augmented by the 12 % of the peptides ( 9 , 12 , 13 , 32 ) that display a bathochromic Soret shift only (UV/Vis group 1). Peptide 32 , in addition, also displayed a mixed state in both Raman and EPR spectroscopy . This finding allows the postulate that a Soret band shift might be indicative of a certain proportion of hexacoordination in 1:1 (heme/peptide) mixtures.…”

Section: Resultsmentioning

confidence: 99%

“…The observations of mixtures of penta-and hexacoordinated complexes for 11 and 30 are consistent with EPR data from an earlier study. [18] Not all of the peptides providing af urthert rifunctional amino acid display hexacoordinated complex geometries. For example, peptides 15 and 27 each showedapentacoordinated state.…”

Section: Investigation Of Complex Geometry By Resonance Raman Spectromentioning

confidence: 99%

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Role of the Chemical Environment beyond the Coordination Site: Structural Insight into Fe^III Protoporphyrin Binding to Cysteine‐Based Heme‐Regulatory Protein Motifs

et al. 2015

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The importance of heme as a transient regulatory molecule has become a major focus in biochemical research. However, detailed information about the molecular basis of transient heme-protein interactions is still missing. We report an in-depth structural analysis of Fe(III) heme-peptide complexes by a combination of UV/Vis, resonance Raman, and 2D-NMR spectroscopic methods. The experiments reveal insights both into the coordination to the central iron ion and into the spatial arrangement of the amino acid sequences interacting with protoporphyrin IX. Cysteine-based peptides display different heme-binding behavior as a result of the existence of ordered, partially ordered, and disordered conformations in the heme-unbound state. Thus, the heme-binding mode is clearly the consequence of the nature and flexibility of the residues surrounding the iron ion coordinating cysteine. Our analysis reveals scenarios for transient binding of heme to heme-regulatory motifs in proteins and demonstrates that a thorough structural analysis is required to unravel how heme alters the structure and function of a particular protein.

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Section: Investigation Of Complex Geometry By Resonance Raman Spectrosupporting

confidence: 90%

Section: Nmr Studies Of Selected Heme-binding Peptidesmentioning

confidence: 52%

Section: Resultsmentioning

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Section: Investigation Of Complex Geometry By Resonance Raman Spectromentioning

confidence: 99%

See 3 more Smart Citations

Role of the Chemical Environment beyond the Coordination Site: Structural Insight into Fe^III Protoporphyrin Binding to Cysteine‐Based Heme‐Regulatory Protein Motifs

et al. 2015

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The pH‐Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α‐Helical Metalloprotein

et al. 2020

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De Novo metalloprotein design assesses the relationship between metal active site architecture and catalytic reactivity. Herein, we use an α‐helical scaffold to control the iron coordination geometry when a heme cofactor is allowed to bind to either histidine or cysteine ligands, within a single artificial protein. Consequently, we uncovered a reversible pH‐induced switch of the heme axial ligation within this simplified scaffold. Characterization of the specific heme coordination modes was done by using UV/Vis and Electron Paramagnetic Resonance spectroscopies. The penta‐ or hexa‐coordinate thiolate heme (9≤pH≤11) and the penta‐coordinate imidazole heme (6≤pH≤8.5) reproduces well the heme ligation in chloroperoxidases or cyt P450 monooxygenases and peroxidases, respectively. The stability of heme coordination upon ferric/ferrous redox cycling is a crucial property of the construct. At basic pHs, the thiolate mini‐heme protein can catalyze O2 reduction when adsorbed onto a pyrolytic graphite electrode.

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The pH‐Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α‐Helical Metalloprotein

et al. 2020

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Spectroscopic studies on peptides and proteins with cysteine-containing heme regulatory motifs (HRM)

Cited by 25 publications

References 28 publications

Role of the Chemical Environment beyond the Coordination Site: Structural Insight into Fe^III Protoporphyrin Binding to Cysteine‐Based Heme‐Regulatory Protein Motifs

Role of the Chemical Environment beyond the Coordination Site: Structural Insight into Fe^III Protoporphyrin Binding to Cysteine‐Based Heme‐Regulatory Protein Motifs

The pH‐Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α‐Helical Metalloprotein

The pH‐Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α‐Helical Metalloprotein

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Spectroscopic studies on peptides and proteins with cysteine-containing heme regulatory motifs (HRM)

Cited by 25 publications

References 28 publications

Role of the Chemical Environment beyond the Coordination Site: Structural Insight into FeIII Protoporphyrin Binding to Cysteine‐Based Heme‐Regulatory Protein Motifs

Role of the Chemical Environment beyond the Coordination Site: Structural Insight into FeIII Protoporphyrin Binding to Cysteine‐Based Heme‐Regulatory Protein Motifs

The pH‐Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α‐Helical Metalloprotein

The pH‐Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α‐Helical Metalloprotein

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Product

Resources

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Role of the Chemical Environment beyond the Coordination Site: Structural Insight into Fe^III Protoporphyrin Binding to Cysteine‐Based Heme‐Regulatory Protein Motifs

Role of the Chemical Environment beyond the Coordination Site: Structural Insight into Fe^III Protoporphyrin Binding to Cysteine‐Based Heme‐Regulatory Protein Motifs