Evolution was Chemically Constrained

Williams, R. J. P.; Silva, João J. R. Fraústo da

doi:10.1006/jtbi.2003.3152

Cited by 125 publications

(99 citation statements)

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“…As R. J. Williams (91,92) and Robert Crichton (93,94) have emphasized, the common era "metallome" is, in essence, the art of the possible, and for redox-active metal ions like iron and copper, it is the art of what is possible in a tidal pool containing 260 M dissolved O 2 . Starting ϳ2.4 gigayears before the common era (95,96), the redox potential of the geosphere began its slow oxidation from negative (Ϫ400 mV as a lower limit) to positive (ϩ400 mV as an upper limit), and the dominant redoxactive first-row transition metal dissolved in the oceans went from Fe(II) to Cu(II).…”

Section: The Why Of Redox Cyclingmentioning

confidence: 99%

Redox Cycling in Iron Uptake, Efflux, and Trafficking

Kosman

2010

Journal of Biological Chemistry

106

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Aerobic organisms are faced with a dilemma. Environmental iron is found primarily in the relatively inert Fe(III) form, whereas the more metabolically active ferrous form is a strong pro-oxidant. This conundrum is solved by the redox cycling of iron between Fe(III) and Fe(II) at every step in the iron metabolic pathway. As a transition metal ion, iron can be "metabolized" only by this redox cycling, which is catalyzed in aerobes by the coupled activities of ferric iron reductases (ferrireductases) and ferrous iron oxidases (ferroxidases).Following the first crystallization of a protein, jack bean urease, reported by Sumner in 1926 (1), the evolution of protein chemistry remained a slow process, hampered by limitations in techniques for protein resolution and analysis. Not surprisingly, many proteins obtained in relatively pure form were those with prosthetic metal ion groups that imparted a visible absorbance to guide the purification. Some were copper proteins whose Cu(II) spectral properties gave their protein host a greenish blue to bright blue hue. Two of these were from mammalian whole blood: hemocuprein (cupric species from erythrocytes, superoxide dismutase) and ceruloplasmin (cerulean blue species from plasma). Superoxide dismutase was first isolated in 1938 by Mann and Keilin (5); Cp 2 was first isolated in 1948 by Holmberg and Laurell (6). Both proteins play essential roles in aerobic homeostasis. In the case of ceruloplasmin and the other copper proteins that share its substrate specificity, this role is to manage the redox state of iron in the metabolism of this essential yet potentially cytotoxic transition metal ion. These proteins, all of which are members of the MCO family (7-9), and the mechanism by which they provide this function are a focus of this minireview.

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Section: The Why Of Redox Cyclingmentioning

confidence: 99%

Redox Cycling in Iron Uptake, Efflux, and Trafficking

Kosman

2010

Journal of Biological Chemistry

106

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“…Within the cell, metals compete for protein binding sites; hence, extensive protein networks involving transporters and metalsensing regulatory proteins are required to maintain the proper subcellular concentrations of each element, and in some cases directly shuttle each metal to its requisite metalloprotein in the proper cellular compartment (1,5,6). It has been hypothesized that the establishment of a metal homeostasis system is required for distinct phylotypes of cells to develop (7).…”

mentioning

confidence: 99%

“…Environmentally, for similar fundamental chemical reasons, the shifts in global redox state hypothesized to have occurred over the past 4.5 billion years (3,7,8) greatly influenced tracemetal abundance. Specifically, the anoxic and reducing Archean ocean would have been enriched in Fe, Mn, and Co, yet low in Cu, Zn, and Mo (8,9).…”

mentioning

confidence: 99%

History of biological metal utilization inferred through phylogenomic analysis of protein structures

Dupont

Butcher

Valas³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

286

248

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The fundamental chemistry of trace elements dictates the molecular speciation and reactivity both within cells and the environment at large. Using protein structure and comparative genomics, we elucidate several major influences this chemistry has had upon biology. All of life exhibits the same proteome size-dependent scaling for the number of metal-binding proteins within a proteome. This fundamental evolutionary constant shows that the selection of one element occurs at the exclusion of another, with the eschewal of Fe for Zn and Ca being a defining feature of eukaryotic proteomes. Early life lacked both the structures required to control intracellular metal concentrations and the metal-binding proteins that catalyze electron transport and redox transformations. The development of protein structures for metal homeostasis coincided with the emergence of metal-specific structures, which predominantly bound metals abundant in the Archean ocean. Potentially, this promoted the diversification of emerging lineages of Archaea and Bacteria through the establishment of biogeochemical cycles. In contrast, structures binding Cu and Zn evolved much later, providing further evidence that environmental availability influenced the selection of the elements. The late evolving Zn-binding proteins are fundamental to eukaryotic cellular biology, and Zn bioavailability may have been a limiting factor in eukaryotic evolution. The results presented here provide an evolutionary timeline based on genomic characteristics, and key hypotheses can be tested by alternative geochemical methods.Archean-Proterozoic | biogeochemistry | bioinorganic chemistry | evolution | metal homeostasis M etalloproteins contain one or more ions of an inorganic element in their 3D structure and are said to comprise 30% of all proteins (1). Many biological pathways contain at least one metalloenzyme (2) and consequently require Mg, K, Ca, Fe, Mn, and Zn to sustain life (3). Other elements, like Cu, Mo, Ni, Se, and Co, are required by many-though not all-organismal lineages, and the utilization of trace elements varies greatly between species (3). The different elements have a range of affinities for most coordinating environments in the order Mg +2 /Ca +2 < Mn +2 < Fe +2 < Co +2 < Ni +2 < Cu +2 ∼Zn +2 , an equilibrium series known as the Irving-Williams Series (4). This array of outer-sphere chemistry provides significant catalytic diversity, yet has consequences for both biological and environmental chemistry. Within the cell, metals compete for protein binding sites; hence, extensive protein networks involving transporters and metalsensing regulatory proteins are required to maintain the proper subcellular concentrations of each element, and in some cases directly shuttle each metal to its requisite metalloprotein in the proper cellular compartment (1, 5, 6). It has been hypothesized that the establishment of a metal homeostasis system is required for distinct phylotypes of cells to develop (7).Environmentally, for similar fundamental chemical reasons, the...

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“…But if we assume conservatively that the pH was around 6 (CO 2 atmosphere), and that it was buffered around H 2 S/SO 4 2-, then the redox would approximate -175 mV, whereas at present it is positive, up to general values of 4.0 Eh . This means that, successively, different elements became involved in the biochemistry of the membranes, as well as in that of the cytosol (Anbar and Knoll 2002;Williams and Fraústo da Silva 2003;Hengeveld and Fedonkin in preparation). However, they could have replaced each other to some extent, but never completely.…”

Section: Ecological Aspects: Elemental and Redox Evolution Of The Envmentioning

confidence: 99%

“…Geochemical observations (e.g. Anbar and Knoll 2002;Williams and Fraústo da Silva 2003) indicate that the required elements were available at the time, but also that, over time, they gradually became exhausted, forcing the system to adapt in a predictive way . Also, energy from a stronger UV radiation generated by an active young Sun, in the absence of a filtering ozone layer continually oxidized ferrous iron, Fe 3+ , to ferric iron, Fe 2+ (Braterman et al 1983).…”

Section: Empirical Versus Deductive Approachesmentioning

confidence: 99%

Two Approaches to the Study of the Origin of Life

Hengeveld

2007

Acta Biotheor

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This paper compares two approaches that attempt to explain the origin of life, or biogenesis. The more established approach is one based on chemical principles, whereas a new, yet not widely known approach begins from a physical perspective. According to the first approach, life would have begun with-often organic-compounds. After having developed to a certain level of complexity and mutual dependence within a non-compartmentalised organic soup, they would have assembled into a functioning cell. In contrast, the second, physical type of approach has life developing within tiny compartments from the beginning. It emphasises the importance of redox reactions between inorganic elements and compounds found on two sides of a compartmental boundary. Without this boundary, ''life'' would not have begun, nor have been maintained; this boundary-and the complex cell membrane that evolved from it-forms the essence of life.

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Evolution was Chemically Constrained

Cited by 125 publications

References 10 publications

Redox Cycling in Iron Uptake, Efflux, and Trafficking

Redox Cycling in Iron Uptake, Efflux, and Trafficking

History of biological metal utilization inferred through phylogenomic analysis of protein structures

Two Approaches to the Study of the Origin of Life

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