Purification of the nickel protein carbon monoxide dehydrogenase of <i>Clostridium thermoaceticum</i>

Diekert, Gabriele; Ritter, Maria

doi:10.1016/0014-5793(83)80338-x

Cited by 62 publications

(24 citation statements)

References 8 publications

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“…Although CODH was indeed very oxygen sensitive, it was not sensitive to light or heat and, when purified and stored under strictly anaerobic conditions, the enzyme was remarkably stable. The CODHs from M. thermoacetica [73, 77] and Acetobacterium woodii [78] were characterized as two-subunit nickel-iron-sulfur metalloenzymes. However, the role of CODH in the acetyl-CoA pathway remained obscure.…”

Section: Importance Of the Wood-ljungdahl Pathwaymentioning

confidence: 99%

Acetogenesis and the Wood–Ljungdahl pathway of CO2 fixation

Ragsdale

Pierce

2008

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

1,014

816

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I. SummaryConceptually, the simplest way to synthesize an organic molecule is to construct it one carbon at a time. The Wood-Ljungdahl pathway of CO 2 fixation involves this type of stepwise process. The biochemical events that underlie the condensation of two one-carbon units to form the two-carbon compound, acetate, have intrigued chemists, biochemists, and microbiologists for many decades. We begin this review with a description of the biology of acetogenesis. Then, we provide a short history of the important discoveries that have led to the identification of the key components and steps of this usual mechanism of CO and CO 2 fixation. In this historical perspective, we have included reflections that hopefully will sketch the landscape of the controversies, hypotheses, and opinions that led to the key experiments and discoveries. We then describe the properties of the genes and enzymes involved in the pathway and conclude with a section describing some major questions that remain unanswered.

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Section: Importance Of the Wood-ljungdahl Pathwaymentioning

confidence: 99%

Acetogenesis and the Wood–Ljungdahl pathway of CO2 fixation

Ragsdale

Pierce

2008

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

1,014

816

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“…Klucas et al (1983), Dalton et al (1985), Soom et al (1993) (continued) Helicobacter pylori Olson et al (2001), Mehta et al (2003) Clostridium thermoaceticum Drake et al (1980), Ragsdale (2002) Methanobacterium thermoautotrophicum , Tersteegen and Hedderich (1999) Alcaligenes eutrophus Friedrich et al (1982) Hammel et al (1984) Clostridium thermoaceticum , Diekert and Ritter (1983), Ragsdale et al (1983aRagsdale et al ( , 1985 Rhodospirillum rubrum Bonam and Ludden (1987) …”

Section: Chromatium Vinosummentioning

confidence: 99%

Essential Roles and Hazardous Effects of Nickel in Plants

Ahmad

Ashraf²

2011

Reviews of Environmental Contamination and Toxicology

140

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With the world's ever increasing human population, the issues related to environmental degradation of toxicant chemicals are becoming more serious. Humans have accelerated the emission to the environment of many organic and inorganic pollutants such as pesticides, salts, petroleum products, acids, heavy metals, etc. Among different environmental heavy-metal pollutants, Ni has gained considerable attention in recent years, because of its rapidly increasing concentrations in soil, air, and water in different parts of the world. The main mechanisms by which Ni is taken up by plants are passive diffusion and active transport. Soluble Ni compounds are preferably absorbed by plants passively, through a cation transport system; chelated Ni compounds are taken up through secondary, active-transport-mediated means, using transport proteins such as permeases. Insoluble Ni compounds primarily enter plant root cells through endocytosis. Once absorbed by roots, Ni is easily transported to shoots via the xylem through the transpiration stream and can accumulate in neonatal parts such as buds, fruits, and seeds. The Ni transport and retranslocation processes are strongly regulated by metal-ligand complexes (such as nicotianamine, histidine, and organic acids) and by some proteins that specifically bind and transport Ni. Nickel, in low concentrations, fulfills a variety of essential roles in plants, bacteria, and fungi. Therefore, Ni deficiency produces an array of effects on growth and metabolism of plants, including reduced growth, and induction of senescence, leaf and meristem chlorosis, alterations in N metabolism, and reduced Fe uptake. In addition, Ni is a constituent of several metallo-enzymes such as urease, superoxide dismutase, NiFe hydrogenases, methyl coenzyme M reductase, carbon monoxide dehydrogenase, acetyl coenzyme-A synthase, hydrogenases, and RNase-A. Therefore, Ni deficiencies in plants reduce urease activity, disturb N assimilation, and reduce scavenging of superoxide free radical. In bacteria, Ni participates in several important metabolic reactions such as hydrogen metabolism, methane biogenesis, and acetogenesis. Although Ni is metabolically important in plants, it is toxic to most plant species when present at excessive amounts in soil and in nutrient solution. High Ni concentrations in growth media severely retards seed germinability of many crops. This effect of Ni is a direct one on the activities of amylases, proteases, and ribonucleases, thereby affecting the digestion and mobilization of food reserves in germinating seeds. At vegetative stages, high Ni concentrations retard shoot and root growth, affect branching development, deform various plant parts, produce abnormal flower shape, decrease biomass production, induce leaf spotting, disturb mitotic root tips, and produce Fe deficiency that leads to chlorosis and foliar necrosis. Additionally, excess Ni also affects nutrient absorption by roots, impairs plant metabolism, inhibits photosynthesis and transpiration, and causes ultrastructural modificat...

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“…With partially purified (14-fold) enzyme of M. thermoacetica, Harland Wood's lab subsequently showed, in 1980, that nickel and CO dehydrogenase activity cochromatograph in polyacrylamide gels (46). Final evidence that CO dehydrogenase is a nickel enzyme was then provided at the end of 1982, when the enzyme was purified to apparent homogeneity (40,122). The heterodimeric enzyme complex contained two to three nickel atoms per mol.…”

Section: Nickel In Carbon Monoxide Dehydrogenase (1979)mentioning

confidence: 99%

My Lifelong Passion for Biochemistry and Anaerobic Microorganisms

Thauer

2015

Annu. Rev. Microbiol.

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Early parental influence led me first to medical school, but after developing a passion for biochemistry and sensing the need for a deeper foundation, I changed to chemistry. During breaks between semesters, I worked in various biochemistry labs to acquire a feeling for the different areas of investigation. The scientific puzzle that fascinated me most was the metabolism of the anaerobic bacterium Clostridium kluyveri, which I took on in 1965 in Karl Decker's lab in Freiburg, Germany. I quickly realized that little was known about the biochemistry of strict anaerobes such as clostridia, methanogens, acetogens, and sulfate-reducing bacteria and that these were ideal model organisms to study fundamental questions of energy conservation, CO 2 fixation, and the evolution of metabolic pathways. My passion for anaerobes was born then and is unabated even after 50 years of study.

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Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum

Abstract: The carbon monoxide dehydrogenase was purified from Clostridium thermoaceticum to apparent homogeneity. The 120‐fold purified enzyme with app. M r 250000 had a nickel content of 10 ± 2 μmol Ni/protein.

Cited by 62 publications

References 8 publications

Acetogenesis and the Wood–Ljungdahl pathway of CO2 fixation

Acetogenesis and the Wood–Ljungdahl pathway of CO2 fixation

Essential Roles and Hazardous Effects of Nickel in Plants

My Lifelong Passion for Biochemistry and Anaerobic Microorganisms

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