Baeckvall J.-E. (ed.) Modern Oxidation Methods

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mutants lead to a reversal of enantioselectivity in the case of regioisomer 9

(Scheme 10.2).

Advances in Regeneration Systems of BVMOs Additional contributions to the

proliferation of the Baeyer-Villiger biotransformation platform is the combination

of the catalytic activity of a redox biocatalyst with concomitant coenzyme recycling in a

single fusion protein, reported by Mihovilovic and Fraaije (Scheme 10.3) [102].

This self-sufﬁcient two-in-one redox biocatalyst enables the use of phosphite

(HPO

2

) as an inexpensive and sacriﬁcial electron donor, and does not require an

additional catalytic entity for coenzyme recycling. As model BVMOs, PAMO,

CHMO, and CPMO were selected. No inhibition of the activity of either the BVMO

or phosphite dehydrogenase (PTDH) by the substrate or product of the other subunit

could be observed.

The use of expensive stoichiometric amounts of NADPH or complicated regen-

eration systems (Scheme 10.4 A) can be avoided by employing light as a source of

(R)-6

(

)

-6

(R), 54% ee

(S), 79% ee

CHMO-

mutants

Scheme 10.1 Directed evolution of cyclohexanone monooxygenases (CHMOs) improves

enantioselectivety in Baeyer-Villiger reactions.

NADPH,H

PAMO-mutants

rac-7

(1S,5R)-8

(1S,5R)-9

(1R,5S)-8

(

1R ,5S

)

-9

Scheme 10.2 PAMO-mutants with high activity and enantioselectivity in the oxidative kinetic

resolution of bicyclic ketone 7.

10.3 Oxidation of Ketones

363

energy (Scheme 10.4 B). In 2007, Reetz and coworkers devised and implemented

experimentally for the ﬁrst time a catalytic scheme for a light-driven ﬂavin-dependent

enzymatic reaction, using EDTA as a reservoir of electrons [103].

As the ﬂavin-dependent enzyme, a mutant of phenylacetone monooxygenase,

PAMO-P3, was chosen [104], which had previously been engineered to catalyze the

enantioselective BV reaction of substituted ketones. The unnatural regeneration

conditions did not impair the inherent stereoselectivity of PAMO-P3, suggesting an

unaltered mechanism of the actual oxidation reaction. The present light-driven BV

reaction is expected to work just as well using other ﬂavin-dependent BVMOs such as

CHMO, which accepts a broader range of substrates.

Despite their efﬁciency and many successes, the bioreagents discussed so far

do not fulﬁll all the needs of synthetic chemistry. There are still a lot of substrates that

NADPH NADP

Pho sp hitePosphate

BVMO

PTDH

Scheme 10.3 Coenzyme regeneration by CRE/BVMO fusion enzymes.

NADP

NADPH

E-FAD

red

E-FAD

BVMOGlucose Dehydrogenase

β-D-glucose

D-glucono-

1,5-lactone

NADP

NADP H

E-FAD

red

E-FAD

BVMO

EDTA

decompo sition

Products

light

(A)

(B)

Scheme 10.4 Comparison of the conventional regeneration of a Baeyer-Villiger monooxygenase

(BVMO, e.g., PAMO) for catalysis through enzymatic regeneration of NADPH (A) and the novel

simplified light-driven pathway using a flavin (B).

364

10 Oxidation of Carbonyl Compounds

are not accepted by any of the currently available BVMOs. In other cases, the regio-

and enantio-selectivities of the reactions are unacceptably low. While the number of

recombinant BVMOs has increased vastly over the past few years, there is still a

demand for other BVMOs to expand the biocatalytic diversity. To meet this demand

new BVMOs have to be discovered or engineered by enzyme redesign. This truly

illustrates the need for a large library of BVMOs to meet the demand for enantio-

and/or regioselective reactions.

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369

Manganese-Catalyzed Oxidation with Hydrogen Peroxide

Wesley R. Browne, Johannes W. de Boer, Dirk Pijper, Jelle Brinksma,

Ronald Hage, and Ben L. Feringa

11.1

Introduction

Oxidation reactions are among the most important synthetic transformations in

organic chemistry [1] and offer core methods for the introduction and modiﬁcation of

functional groups [2]. Despite its central role, the continued use of stoichiometric

oxidants including nitric acid, chromic acid and its derivatives, alkyl hydroperoxides,

permanganate, osmium tetroxide, hypochlorite bleach, hydrogen peroxide, and

peracids is remarkable considering the extensive use of catalytic methods in most

other areas of chemical synthesis and the high costs, formation of toxic waste, and

low atom efﬁciency that the use of stoichiometric methods involves. The increasing

role that catalysis plays in organic chemistry in general and the ever-increasing

consideration given to environmental aspects provide a strong incentive to develop

sustainable catalytic alternatives to stoichiometric reagents [3–6].

Oxidations with molecular dioxygen [7], the primary oxidant in biologic systems [8],

are desirable and indeed already employed in large-scale industrial processes [9],

albeit being frequently hampered by low conversion, modest selectivity, and safety

issues. Although both oxygen atoms of O

can be transferred in dioxygenation or

reactions with singlet dioxygen, frequently stoichiometric amounts of a reducing

agent are required to convert one of the oxygen atoms of O

to water. Hydrogen

peroxide is particularly attractive, as it has a high active-oxygen content, yields H

as its only waste product, and is a relatively low-cost oxidant. One of the problems

frequently encountered in metal-catalyzed oxidations with hydrogen peroxide is

the concomitant decomposition of H

(catalase activity), which often requires that

a large excess of H

is employed to reach full conversion [10]. Application of

[11], in particular to metal-catalyzed epoxidations in general [12] and green

oxidations [4, 5], have been reviewed elsewhere. In this chapter we will focus on

Mn-catalyzed oxidations with H

KMnO

, the archetypal stoichiometric manganese based oxidant, still retains its

place as a classic oxidation reagent in nearly every introductory course on organic

371

chemistry [13, 14]. Ironically, this oxidizing agent is of limited use in practical

synthetic chemistry and is often seen as a tool of last resort. It is only in recent years

that several discoveries have revealed the potential of manganese catalysts for

selective oxidations. This has evolved in part from studies on the structure and

function of Mn-based redox enzymes [15, 16]. In this chapter we will review

biomimetic manganese systems brieﬂy and then proceed to discuss oxidative

transformations with H

catalyzed by Mn complexes in more depth, with special

consideration of mechanistic insights gained over recent years.

11.2

Bio-inspired Manganese Oxidation Catalysts

Manganese can frequently be found in the catalytic redox center of several en-

zymes [10, 15] including superoxide dismutases [17], catalases [18], and the dioxygen-

evolving complex photosystem II (PSII) [19, 20]. Superoxide (O



), a radical harmful

to living organisms, is the product of the one-electron reduction of dioxygen [21].

Its high reactivity requires that it is converted to less reactive species rapidly.

Superoxide dismutase metalloenzymes catalyze the dismutation of the superoxide



) to dioxygen (O

) and hydrogen peroxide (H

) [22]. The latter product can be

disproportionated by catalase enzymes to water and dioxygen (see above). Superoxide

dismutase (SOD) enzymes can be classiﬁed into two major structural families;

copper-zinc SOD and manganese or iron SOD [21, 23]. The active site of manganese

SOD contains a mononuclear ﬁve-coordinate Mn

III

-ion bound to three histidines,

one aspartate residue, and one water or hydroxide ligand. The mechanism of the

catalytic conversion of superoxide to dioxygen starts by binding of the superoxide

radical anion to the Mn

III

-monomer leading to the reduction to Mn

and oxidation of

superoxide to dioxygen [17, 24]. Subsequently, the catalytic cycle is closed by binding

of a second superoxide to the Mn

-ion resulting in the oxidation to Mn

III

and

reduction of the superoxide anion to H

In photosystem II (PSII), located in the thylakoid membrane of chloroplasts in

green plants, algae, and a number of cyanobacteria, two water molecules are oxidized

to dioxygen, that is, water splitting [19]. PSII consists of light-harvesting pigments,

a water oxidation center (WOC), and electron transfer components [19]. Based on

detailed spectroscopic analyses, it has been recognized that a tetranuclear Mn cluster

is the active catalyst for the dioxygen evolution, and this assignment is supported by

X-ray analysis [25]. Although the detailed mechanism of the water oxidation com-

ponent remains to be elucidated fully, current opinion highlights the cooperativity

of the manganese ions in the cluster with calcium in achieving the transfer of four

electrons and liberation of dioxygen [26].

Manganese-containing catalases have been isolated from three species of bacteria;

Lactobacillus plantarum [27], Thermus thermophilus [28], and Thermoleophilum

album [18]. X-ray crystallographic structure analysis [29] has shown that these

catalases contain a dinuclear manganese core. During catalysis, the dinuclear

manganese active site cycles between the Mn

- and Mn

III

oxidation states [30].

372

11 Manganese-Catalyzed Oxidation with Hydrogen Peroxide