ผ่านทาง ifa-Micronutrients – Windows Live.
Micronutrients for Sustainable Food, Feed, Fibre and Bioenergy Production,
Author(s): Bell, R.W.; Dell, B.
Publisher(s): IFA, Paris, France, December 2008
The publication can be downloaded from IFA’s web site.
IFA : International Fertilizer Industry Association – Micronutrients for Sustainable Food, Feed, Fibre and Bioenergy Production .
To obtain paper copies, contact IFA.
as Fe(III), mostly as phytoferritin, and is reduced to Fe(II) for physiological function in
the cell. Iron is generally incorporated into heme and non-heme proteins. Th e most
well-known heme proteins are the cytochromes, which contain a heme Fe-porphyrin
complex (Marschner, 1995).
In legume nodules, a related class of compounds, the leghemoglobins, regulate
the supply of oxygen to the bacteroids responsible for fi xation of N. Th e bacterial
nitrogenase enzyme, which reduces N2 to NH3, consists of two metalloproteins, the
Fe protein (dinitrogenase reductase) and the FeMo protein (dinitrogenase) (Bosch and
Imperial, 2000).
Other heme proteins are involved in the formation of lignin and suberin (peroxidases),
and the breakdown of H2O2 to water and oxygen (catalases). Th e most common nonheme
proteins contain Fe-S clusters, which serve as cofactors for redox, catalytic and
regulatory functions. Examples of Fe-S proteins are ferredoxin and Fe-SOD. Ferredoxin
is an electron carrier assisting enzymes involved in the reduction of nitrite (NO2
-) and
sulphite (SO3
2-), and biological N2 fi xation, and is an essential component of the electron
transport pathway in photosynthesis.
Animals and humans Iron is essential for humans and animals. It plays a central role
in metabolic processes involving oxygen transport and storage as well as oxidative
metabolism and cellular growth. About 85 % of body Fe is a constituent of two heme
proteins: hemoglobin, essential for transferring oxygen in the blood from the lungs
to tissues; and myoglobin, the oxygen store in muscles. A number of other heme
proteins are enzymes and include the cytochromes involved in energy production
in the mitochondria, and peroxidases that degrade reactive by-products of oxygen
metabolism.
Non-heme proteins can store and transport Fe (ferritin, transferritin) or function as
enzymes (metallofl avoproteins, Fe-S proteins, ribonucleotide reductase). Examples of
Fe-S proteins are NADH dehydrogenase and succinate dehydrogenase that play roles in
energy metabolism (Yip and Dallman, 1996). In adult men, about one third of the total
body Fe is stored Fe, whereas, in women, storage accounts for about one eighth of total
body Fe (Yip and Dallman, 1996). Dietary Fe overload can cause acute Fe poisoning as
the body has no adjustable Fe excretory mechanism (Lynch, 2003a).
Requirements
Plants Critical defi ciency concentrations for Fe in leaves typically range from 50–150
mg Fe/kg although levels may be marginally greater in C4 plants (Marschner, 1995). Iron
defi ciency is common on calcareous and high pH soils due to impaired Fe acquisition
commonly known as ‘lime-induced chlorosis’. Diagnosis of Fe defi ciency by plant
analysis is limited, since there is oft en no relationship between total leaf Fe content and
defi ciency symptoms. Moreover, Fe concentrations in chlorotic leaves are frequently
greater than those in healthy green leaves. Th is phenomenon, known as the ‘chlorosis
paradox’, is caused by inactivation of Fe in the leaf.
13.874246
100.669851