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32  structures 309  species 1  interaction 416  sequences 3  architectures

Family: HIPIP (PF01355)

Summary: High potential iron-sulfur protein

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High potential iron-sulfur protein Edit Wikipedia article

High potential iron-sulfur protein
PDB 1hpi EBI.jpg
Structure of the oxidized high-potential iron-sulfur protein.[1]
Identifiers
Symbol HIPIP
Pfam PF01355
InterPro IPR000170
PROSITE PDOC00515
SCOP 1hpi
SUPERFAMILY 1hpi
OPM superfamily 124
OPM protein 1hpi

High potential iron-sulfur proteins (HIPIP)[2] are a specific class of high-redox potential 4Fe-4S ferredoxins that functions in anaerobic electron transport and which occurs in photosynthetic bacteria and in Paracoccus denitrificans. The HiPIPs are small proteins which show significant variation in their sequences, their sizes (from 63 to 85 amino acids), and in their oxidation- reduction potentials. As shown in the following schematic representation the iron-sulfur cluster is bound by four conserved cysteine residues.

                          [ 4Fe-4S cluster]
                          | |       |     |
       xxxxxxxxxxxxxxxxxxxCxCxxxxxxxCxxxxxCxxxx

'C': conserved cysteine involved in the binding of the iron-sulfur cluster.

[Fe4S4] clusters

The [Fe4S4] clusters are abundant cofactors of metalloproteins.[3] They participate in electron-transfer sequences. The core structure for the [Fe4S4] cluster is a cube with alternating Fe and S vertices. These clusters exist in two oxidation states with a small structural change. Two families of [Fe4S4] clusters are known: the ferredoxin (Fd) family and the high-potential iron–suflur protein (HiPIP) family. Both HiPIP and Fd share the same resting state: [Fe4S4]2+, which have the same geometric and spectroscopic features. Differences arise when it comes to their active state: HiPIP forms by oxidation to [Fe4S4]3+, and Fd is formed by reduction to [Fe4S4]+.

equations on Fd and HiPIP

The different oxidation states are explained by the proteins that combined with the [Fe4S4] cluster. Analysis from crystallographic data suggests that HiPIP is capable of preserving its higher oxidation state by forming fewer hydrogen bonds with water. The characteristic fold of the proteins wraps the [Fe4S4] cluster in a hydrophobic core, only being able to form about five conserved H-bond to the cluster ligands from the backbone. In contrast, the protein associated with the Fd's allows these clusters to contact solvent resulting in 8 protein H-bonding interactions. The protein binds Fd via conserved CysXXCysXXCys structure (X stands for any amino acid).[4] Also, the unique protein structure and dipolar interactions from peptide and intermolecular water contribute to shielding the [Fe4S4]3+ cluster from the attack of random outside electron donors, which protects itself from hydrolysis.

Synthetic analogues

HiPIP analogues can be synthesized by ligand exchange reactions of [Fe4S4{N(SiMe3)2}4]− with 4 equiv of thiols (HSR) as follows:

[Fe4S4{N(SiMe3)2}4]− + 4RSH → [Fe4S4(SR)4]− + 4 HN(SiMe3)2

The precursor cluster [Fe4S4{N(SiMe3)2}4]− can be synthesized by one-pot reaction of FeCl3, NaN(SiMe3)2, and NaSH. The synthesis of HiPIP analogues can help people understand the factors that cause variety redox of HiPIP.[5]

Biochemical reactions

HiPIPs take part in many oxidizing reactions in creatures, and are especially known with photosynthetic anaerobic bacteria, such as Chromatium, and Ectothiorhodospira. HiPIPs are periplasmic proteins in photosynthetic bacteria. They play a role of electron shuttles in the cyclic electron flow between the photosynthetic reaction center and the cytochrome bc1 complex. Other oxidation reactions HiPIP involved include catalyzing Fe(II) oxidation, being electron donor to reductase and electron accepter for some thiosulfate-oxidizing enzyme.[6]

References

  1. ^ Benning MM, Meyer TE, Rayment I, Holden HM (1994). "Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated from Ectothiorhodospira vacuolata". Biochemistry 33 (9): 2476–2483. doi:10.1021/bi00175a016. PMID 8117708. 
  2. ^ Breiter DR, Meyer TE, Rayment I, Holden HM (1991). "The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution". The Journal of biological chemistry 266 (28): 18660–18667. PMID 1917989. 
  3. ^ Jr, Perrin; T., Ichive (2013). "Identifying sequence determinants of reduction potentials of metalloproteins". Biological Inorganic Chemistry 18 (6): 599–608. doi:10.1007/s00775-013-1004-6. 
  4. ^ Dey, Abhishek; Jr, Francis; Adams, Michael; Babini, Elena; Takahashi, Yasuhiro; Fukuyama, Keiichi; Hodgson, Keith; Hedman, Britt; Solomon, Edward (2007). "Solvent Tuning of Electronchemical Potentials in the Active Sites of HiPIP Versus Ferredoxin". Science 318 (5855): 1464–1468. doi:10.1126/science.1147753. PMID 18048692. 
  5. ^ Ohki, Yasuhiro; Tanifuji, Kazuki; Yamada, Norihiro; Imada, Motosuke; Tajima, Tomoyuki; Tatsumi, Kazujuki (2011). "Synthetic analogues of [Fe4S4(Cys)3(His)] in hydrogenases and [Fe4S4(Cys)4] in HiPIP derived from all-ferric [Fe4S4{N(SiMe3)2}4]". Proceedings of the National Academy of Sciences of the United States of America 108 (31): 12635–12640. doi:10.1073/pnas.1106472108. 
  6. ^ Valentine, Joan; Bertini, Ivano; Gray, Harry; Stiefel, Edward (2006-10-30). Biological Inorganic Chemistry: Structure and Reactivity (first ed.). ISBN 978-1891389436. 

External links

Further reading

This article incorporates text from the public domain Pfam and InterPro IPR000170

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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Literature references

  1. Breiter DR, Meyer TE, Rayment I, Holden HM; , J Biol Chem 1991;266:18660-18667.: The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution. PUBMED:1917989 EPMC:1917989

  2. Nogi T, Fathir I, Kobayashi M, Nozawa T, Miki K; , Proc Natl Acad Sci U S A 2000;97:13561-13566.: Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum, thermostability and electron transfer. PUBMED:11095707 EPMC:11095707


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000170

High potential iron-sulphur proteins (HiPIP) [PUBMED:1917989, PUBMED:1317860] are a specific class of high-redox potential 4Fe-4S ferredoxins that functions in anaerobic electron transport and which occurs commonly in purple photosynthetic bacteria and in other bacteria, such as Paracoccus denitrificans and Thiobacillus ferrooxidans [PUBMED:14562962].

HiPIPs seem to react by oxidation of [4Fe-4S]2+ to [4Fe-4S]3+

The HiPIPs are small proteins which show significant variation in their sequences, their sizes (from 63 to 85 amino acids), and in their oxidation- reduction potentials. As shown in the following schematic representation the iron-sulphur cluster is bound by four conserved cysteine residues.

                           [4Fe-4S cluster]
                           | |       |     |
        xxxxxxxxxxxxxxxxxxxCxCxxxxxxxCxxxxxCxxxx
'C': conserved cysteine involved in the binding of the iron-sulphur cluster.

Gene Ontology

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Domain organisation

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  Seed
(37)
Full
(416)
Representative proteomes NCBI
(534)
Meta
(45)
RP15
(10)
RP35
(45)
RP55
(70)
RP75
(111)
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  Seed
(37)
Full
(416)
Representative proteomes NCBI
(534)
Meta
(45)
RP15
(10)
RP35
(45)
RP55
(70)
RP75
(111)
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Curation and family details

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Seed source: SCOP
Previous IDs: none
Type: Domain
Author: Bateman A
Number in seed: 37
Number in full: 416
Average length of the domain: 63.90 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 59.18 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.5 21.5
Trusted cut-off 21.5 21.6
Noise cut-off 21.3 21.4
Model length: 66
Family (HMM) version: 13
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Interactions

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HIPIP

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HIPIP domain has been found. There are 32 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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