Proton NMR investigation of the oxidized three-iron clusters in the ferredoxins from the hyperthermophilic archae Pyrococcus furiosus and Thermococcus litoralis.

Proton NMR investigation of the oxidized three-iron clusters in the ferredoxins from the hyperthermophilic archae Pyrococcus furiosus and Thermococcus litoralis.
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对来自超嗜热古菌激烈火球菌和北海热球菌铁氧还蛋白中氧化三铁簇的质子核磁共振研究。

DOI:
10.1021/bi00162a038
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发表时间:
1992
期刊:
影响因子:
2.9
通讯作者:
Adams,MW
Adams,MW
中科院分区:
生物学3区
文献类型:
--
作者:
Busse,SC;LaMar,GN;Yu,LP;Howard,JB;Smith,ET;Zhou,ZH;Adams,MW

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摘要:用核磁共振研究了极端嗜热古细菌激烈火球菌(Pyrococcus furiosus,Pf)和滨海热球菌(Thermococcus litoralis,TV)中铁氧还蛋白(ferredoxins,Fd)的3 Fe形式。一维核Overhauser和二维NOESY和键相关光谱的组合提供了分配的芳香族残基,一个保守的缬氨酸,和三个半胱氨酸的每个协调的集群的信号的位置。在PfFd中Trp 2和Tyr 46之间的偶极接触,以及从不变的苯丙氨酸到不变的缬氨酸和两个Fd中的簇半胱氨酸,证实了这些蛋白质的折叠模式,其非常类似于来自嗜热链球菌Desulfovibro gigas的晶体学表征的铁氧还蛋白。序列特异性分配的掩埋半胱氨酸附近的不变的苯丙氨酸已作出。接触位移的半胱氨酸残基的温度依赖性揭示了一个明显的2:1不对称的磁耦合之间的三个高自旋铁离子,在一个半胱氨酸表现出居里行为,而其他两个半胱氨酸显示anti-Curie行为。这些磁性的合理化定性的基础上的磁耦合方案,其中两个铁耦合产生一个中间自旋2耦合到其余的5=5/2铁,产生总的集群自旋1/2。这种磁不对称似乎是氧化的3Fe簇的特征。PfFd也经历了两种交替形式之间的动态平衡,这两种交替形式在两个配位半胱氨酸的环境中略有不同。对两种铁氧还蛋白中三个半胱氨酸的接触位移模式的分析表明,与独特的铁配位的半胱氨酸不具有相同的序列起源。
Revised Manuscript Received September 24, 1992 abstract: The 3Fe forms of ferredoxins (Fd) from the hyperthermophilic archaebacteria Pyrococcus furiosus (Pf) and Thermococcus litoralis (TV) have been investigated by NMR. A combination of one-dimensional nuclear Overhauser and two-dimensional NOESY and bond correlation spectroscopy provides the assignment of the aromatic residues, one conserved valine, and the location of the signals for each of the three cysteines coordinated to the clusters. Dipolar contacts between the Trp 2 and Tyr 46 in Pf Fd and from an invariant phenylalanine to an invariant valine and a cluster cysteine in both Fd confirm a folding pattern for these proteins that is very similar to that of the crystallographically characterized ferredoxin from themesophile Desulfovibro gigas. The sequence-specific assignment of the buried cysteine near the invariant phenylalanine has been made. The temperature dependence of the contact-shifted cysteinyl residues reveals a distinct 2: 1 asymmetry in the magnetic coupling among the three high-spin ferric ions, in that one cysteine exhibits Curie behavior, while the other two cysteines displayanti-Curie behavior. These magnetic properties are rationalized qualitatively on the basis of a magnetic coupling scheme where two iron couple to yield an intermediate spin of 2 which couples to the remaining 5=5/2 iron to yield the total cluster spin 1/2. This magnetic asymmetry appears to be a characteristic feature of oxidized 3Fe clusters. PfFd also undergoes a dynamic equilibrium between two alternate forms that differ slightlyin the environment of two of the coordinated cysteines. Analysis of the pattern of the contact shifts for the three cysteines in the two ferredoxins suggests that thecysteine coordinated to the unique iron does not have the same sequence origin.
人白细胞明胶特异性蛋白酶的进一步纯化和一些特性。
DOI: 10.1016/0304-4165(82)90375-0
发表时间: 1982
期刊: Biochimica et biophysica acta
影响因子: --
作者:
I. Sopata
通讯作者: I. Sopata
DOI: 10.1172/jci112887
发表时间: 1987-03-01
影响因子: 15.9
作者:
BISSELL, DM;ARENSON, DM;ROLL, FJ
通讯作者: ROLL, FJ
DOI: 10.1016/0076-6879(87)44177-3
发表时间: 1987
影响因子: --
作者:
H. Birkedal‐Hansen
通讯作者: H. Birkedal‐Hansen
DOI: 10.1073/pnas.82.24.8681
发表时间: 1985-12-01
影响因子: 11.1
作者:
FRIEDMAN, SL;ROLL, FJ;BISSELL, DM
通讯作者: BISSELL, DM