An EPR/HYSCORE, Mössbauer, and resonance Raman study of the hydrogenase maturation enzyme HydF: a model for N-coordination to [4Fe–4S] clusters View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-11-17

AUTHORS

Gustav Berggren, Ricardo Garcia-Serres, Xavier Brazzolotto, Martin Clemancey, Serge Gambarelli, Mohamed Atta, Jean-Marc Latour, Heather L. Hernández, Sowmya Subramanian, Michael K. Johnson, Marc Fontecave

ABSTRACT

The biosynthesis of the organometallic H cluster of [Fe–Fe] hydrogenase requires three accessory proteins, two of which (HydE and HydG) belong to the radical S-adenosylmethionine enzyme superfamily. The third, HydF, is an Fe–S protein with GTPase activity. The [4Fe–4S] cluster of HydF is bound to the polypeptide chain through only the three, conserved, cysteine residues present in the binding sequence motif CysXHisX(46-53)HisCysXXCys. However, the involvement of the two highly conserved histidines as a fourth ligand for the cluster coordination is controversial. In this study, we set out to characterize further the [4Fe–4S] cluster of HydF using Mössbauer, EPR, hyperfine sublevel correlation (HYSCORE), and resonance Raman spectroscopy in order to investigate the influence of nitrogen ligands on the spectroscopic properties of [4Fe–4S]2+/+ clusters. Our results show that Mössbauer, resonance Raman, and EPR spectroscopy are not able to readily discriminate between the imidazole-coordinated [4Fe–4S] cluster and the non-imidazole-bound [4Fe–4S] cluster with an exchangeable fourth ligand that is present in wild-type HydF. HYSCORE spectroscopy, on the other hand, detects the presence of an imidazole/histidine ligand on the cluster on the basis of the appearance of a specific spectral pattern in the strongly coupled region, with a coupling constant of approximately 6 MHz. We also discovered that a His-tagged version of HydF, with a hexahistidine tag at the N-terminus, has a [4Fe–4S] cluster coordinated by one histidine from the tag. This observation strongly indicates that care has to be taken in the analysis of data obtained on tagged forms of metalloproteins. More... »

PAGES

75-84

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00775-013-1062-9

DOI

http://dx.doi.org/10.1007/s00775-013-1062-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037063945

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24240692


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16 schema:description The biosynthesis of the organometallic H cluster of [Fe–Fe] hydrogenase requires three accessory proteins, two of which (HydE and HydG) belong to the radical S-adenosylmethionine enzyme superfamily. The third, HydF, is an Fe–S protein with GTPase activity. The [4Fe–4S] cluster of HydF is bound to the polypeptide chain through only the three, conserved, cysteine residues present in the binding sequence motif CysXHisX(46-53)HisCysXXCys. However, the involvement of the two highly conserved histidines as a fourth ligand for the cluster coordination is controversial. In this study, we set out to characterize further the [4Fe–4S] cluster of HydF using Mössbauer, EPR, hyperfine sublevel correlation (HYSCORE), and resonance Raman spectroscopy in order to investigate the influence of nitrogen ligands on the spectroscopic properties of [4Fe–4S]2+/+ clusters. Our results show that Mössbauer, resonance Raman, and EPR spectroscopy are not able to readily discriminate between the imidazole-coordinated [4Fe–4S] cluster and the non-imidazole-bound [4Fe–4S] cluster with an exchangeable fourth ligand that is present in wild-type HydF. HYSCORE spectroscopy, on the other hand, detects the presence of an imidazole/histidine ligand on the cluster on the basis of the appearance of a specific spectral pattern in the strongly coupled region, with a coupling constant of approximately 6 MHz. We also discovered that a His-tagged version of HydF, with a hexahistidine tag at the N-terminus, has a [4Fe–4S] cluster coordinated by one histidine from the tag. This observation strongly indicates that care has to be taken in the analysis of data obtained on tagged forms of metalloproteins.
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22 schema:keywords EPR
23 EPR spectroscopy
24 Fe-S proteins
25 GTPase activity
26 H-cluster
27 HYSCORE spectroscopy
28 HydF
29 HydF.
30 MHz
31 Mössbauer
32 N-coordination
33 N-terminus
34 Raman
35 Raman spectroscopy
36 Raman studies
37 accessory proteins
38 activity
39 analysis
40 analysis of data
41 appearance
42 basis
43 biosynthesis
44 care
45 chain
46 cluster coordination
47 clusters
48 coordination
49 correlation
50 coupling
51 cysteine residues
52 data
53 enzyme
54 form
55 fourth ligand
56 hand
57 hexahistidine tag
58 histidine
59 histidine ligands
60 hydrogenase
61 hyperfine sublevel correlation
62 influence
63 involvement
64 ligands
65 metalloproteins
66 model
67 motif
68 nitrogen ligands
69 observations
70 order
71 organometallic H-cluster
72 patterns
73 polypeptide chain
74 presence
75 properties
76 protein
77 radical S-adenosylmethionine (SAM) enzyme
78 region
79 residues
80 resonance Raman
81 resonance Raman spectroscopy
82 resonance Raman study
83 results
84 sequence motifs
85 specific spectral patterns
86 spectral patterns
87 spectroscopic properties
88 spectroscopy
89 study
90 tagged forms
91 tags
92 version
93 schema:name An EPR/HYSCORE, Mössbauer, and resonance Raman study of the hydrogenase maturation enzyme HydF: a model for N-coordination to [4Fe–4S] clusters
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