The Primary Structure of the Clostridium tartarivorum Ferredoxin, a Heat-stable Ferredoxin

Tanaka, Masaru; Haniu, Mitsuru; Matsueda, Gary R.; Yasunobu, Kerry T.; Himes, Richard H.; Akagi, J. M.; Barnes, Elizabeth M.; Devanathan, T. G.

doi:10.1016/s0021-9258(18)62126-x

Cited by 69 publications

(6 citation statements)

References 15 publications

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“…The latter contains a glutamic acid rather than a glutamine at residue 44 and does not form a salt bridge with His-2. Histidine is reported at residue 2 in thermophilic ferredoxins from C. tartarivorum (Tanaka et al, 1971), C. thermosaccharolyticum (Yasunobu & Tanaka, 1973), and the aerobe, Thermus thermophilus (Sato et al, 1981). Lysine is present at the identical position in the ferredoxins from B. stearothermophilus (Hase et al, 1976) and, as presented here, C. thermoaceticum.…”

Section: Discussionsupporting

confidence: 60%

Complete amino acid sequence of the 4Fe-4S, thermostable ferredoxin from Clostridium thermoaceticum

Elliott¹,

Yang²,

Ljungdahl³

et al. 1982

Biochemistry

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The complete amino acid sequence of the 4Fe-4S ferredoxin from the thermophilic bacterium Clostridium thermoaceticum has been determined. The protein is extremely thermostable and is the only known clostridial ferredoxin to contain a single [4Fe-4S] cluster. The sequence totals 63 residues and includes the first tryptophan (Trp-26) reported for a clostridial ferredoxin, and other amino acids not commonly found in clostridial or clostridial-like ferredoxins: methionine (Met-1), histidine (His-33), arginine (Arg-49), and leucine (Leu-9, -19, and -31). Sequence homology to clostridial and other 8Fe-8S ferredoxins is limited to eight to nine residues at the amino-terminal sulfhydryl grouping (Cys-10, -13, -16, and -20) and two to five residues in the carboxyterminal region. This ferredoxin is, thus, sequentially distinct from all known clostridial ferredoxins and from other bacterial ferredoxins in both the 8Fe-8S and 4Fe-4S classes.

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Section: Discussionsupporting

confidence: 60%

Complete amino acid sequence of the 4Fe-4S, thermostable ferredoxin from Clostridium thermoaceticum

Elliott¹,

Yang²,

Ljungdahl³

et al. 1982

Biochemistry

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“…147 many respects to those reported in the present study. It would be tempting to assert, as we did for S. lividus, the possible importance of glutamic acid substitutions, using as analogies the work on enolase (Barnes & Stellwagen, 1973) and ferredoxin (Tanaka et al, 1971) from thermophilic sources. There is, however, an important difference: the very large deviation in the isoelectric point with C. caldarium C-phycocyanin, an increase of almost 0.4 unit over other reported values for the native protein (MacColl et al, 1974;Kao et al, 1973;.…”

Section: Discussionmentioning

confidence: 96%

Physical-chemical properties of C-phycocyanin isolated from an acido-thermophilic eukaryote, Cyanidium caldarium

Kao

Edwards

Berns

1975

Biochemical Journal

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C-Phycocyanin from an acido-thermophilic eukaryotic alga, Cyanidium caldarium, was characterized with respect to subunit structure, absorption spectrum and fluorescence properties and was found to be similar to C-phycocyanins from mesophilic sources. The pH-dependence of fluorescence polarization and the changes in sedimentation velocity as a function of pH, concentration and temperature indicate the presence of extremely large amounts of unusually stable 19S aggregates. It was not possible to disaggregate this phycocyanin completely to monomer under normal conditions. The amino acid composition is similar to that of phycocyanins from other thermophilic and halophilic sources. The isoelectric point of this C-phycocyanin was 5.11, an unusually high value. The properties of this C-phycocyanin suggest an increase in protein stability as its mode of adaptation to the environmental stress of high temperature.

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“…The C-terminal eight cysteine residues are arranged in a ferrodoxinlike sequence, suggestive of two 4Fe/4S clusters. The best overall similarity is with the ferrodoxin of Clostridium thermosaccharolyticum (Tanaka et al, 1971(Tanaka et al, , 1973. However, as shown in Figure 5, there also exists a similarity with the ferrodoxin domains of mvhB, the gene encoding the polyferredoxin of the MVH (Reeve et (Tanaka et al, 1971(Tanaka et al, , 1973, R. rubrum (Matsubara et al, 1983), mvhB, the "polyferredoxin" (the mvhB gene encodes a protein with six repeating ferredoxin domains) of M. thermoautotrophicum AH (Reeve et al, 1989) and a 3Fe/3S ferredoxin of M. barkeri (Hausinger et al, 1982).…”

Section: Discussionmentioning

confidence: 99%

Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum .DELTA.H

Alex¹,

Reeve²,

Orme‐Johnson³

et al. 1990

Biochemistry

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The genes frhA (1217 bp), frhB (845 bp), and frhG (710 bp) encoding the three known subunits, alpha, beta, and gamma, of the 8-hydroxy-5-deazaflavin (F420) reducing hydrogenase (FRH) from the thermophilic methanogen Methanobacterium thermoautotrophicum delta H have been cloned, sequenced, and shown to be tightly linked, indicative of a single transcriptional unit. The DNA sequence contains a fourth open reading frame, designated frhD (476 bp), encoding a polypeptide (delta) that does not copurify with the active enzyme. Expression of the frh gene cluster in Escherichia coli shows that four polypeptides are synthesized. When analyzed by SDS-PAGE, the proteins migrate with mobilities consistent with their calculated molecular weights. In order to understand the mechanism of H2 oxidation by this enzyme, localization of redox cofactors (Ni, Fe/S, FAD) to specific subunits and information on their structure is needed. This has been hindered due to the refractory nature of the enzyme to denaturation methods needed in order to obtain individual subunits with cofactors intact. In this paper we discuss the possible localization of the redox cofactors as implicated from the DNA-derived protein sequences of the subunits. The amino acid sequences of the subunits of the FRH are compared with those of other Ni-containing hydrogenases, including the methyl viologen reducing hydrogenase (MVH) of M. thermoautotrophicum delta H.

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The Primary Structure of the Clostridium tartarivorum Ferredoxin, a Heat-stable Ferredoxin

Cited by 69 publications

References 15 publications

Complete amino acid sequence of the 4Fe-4S, thermostable ferredoxin from Clostridium thermoaceticum

Complete amino acid sequence of the 4Fe-4S, thermostable ferredoxin from Clostridium thermoaceticum

Physical-chemical properties of C-phycocyanin isolated from an acido-thermophilic eukaryote, Cyanidium caldarium

Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum .DELTA.H

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